Antonina Roll-Mecak, Ph.D.

Senior Investigator, Cell Biology and Biophysics Section
Antonina Roll-Mecak, Ph.D.
Division
Division of Intramural Research
Areas of Interest

Cell Biology of Neurons, Muscle and Glia, and Neurological Disorders

Contact
antonina.roll-mecak@nih.gov
301-402-7353

Antonina grew up surrounded by science and music. After completing her baccalaureate in Mathematics and Physics she studied engineering at Cooper Union in New York City. She fell in love with structural biology after attending a seminar on protein structures at the New York Academy of Science. She enrolled as a graduate student at Rockefeller University to pursue her interest in protein structure and function. She became fascinated by the intricate choreography of the ribosome as it prepares to start protein synthesis and studied this process as a NSF graduate fellow in the lab of Stephen Burley. Her work shed light on the structure and mechanism of the two GTPases, eIF2 and eIF5B, which are involved in delivering the initiator Met-tRNA on the ribosome and facilitating the joining of the small and large ribosomal subunits to commence translation of the mRNA. As she was nearing the end of her Ph.D. she decided that in order to understand protein function she needed to complement her structural biology skills with methods that capture protein dynamics in isolation as well as in the more complex environment of the cell. She decided to join Ron Vale’s lab at UCSF where she was a Damon Runyon fellow and then a Burroughs Wellcome Career Award recipient. While there, she identified spastin as a novel microtubule severing enzyme and used hybrid structural biology methods and light microscopy to shed light on its mechanism of action. Combining her interdisciplinary skills she started her own lab at the National Institutes of Health (NINDS with a joint appointment at NHLBI) focused on the tubulin code. Her lab is deciphering the molecular and cellular mechanism of action of the tubulin code using tools from biophysics, X-ray crystallography, cryo-electron microscopy and tomography, proteomics, cell biology, high-resolution light microscopy and modeling.  She has assembled a diverse team of scientists who draw from the fields of biology, chemistry, and physics.

Education and Training

  • The Cooper Union, B.E. in Chemical Engineering (1992-1996)
  • The Rockefeller University, Ph.D. in Molecular Biophysics with Stephen K. Burley (1996-2002)
  • University of California, San Francisco, postdoctoral fellow with Ronald D. Vale (2003-2009)
 

Awards and Funding

  • The Henry W. Reddick Fund Prize and Medal for meritorious work in mathematics (1996)
  • William C. & Esther Hoffman Beller Fund for merit in engineering studies (1996)
  • The Kosciuszko Foundation Fellowship Grant (1997-1999)
  • National Science Foundation Predoctoral Fellowship (1997 – 2000)
  • Burroughs Wellcome Fund Predoctoral Fellowship (2000 – 2002)
  • Damon Runyon Cancer Research Fund Postdoctoral Fellowship (2003 – 2006)
  • L’Oreal-AAAS For Women in Science Fellowship Award (2006)
  • American Heart Association Scientist Development Award (2006 – 2010; declined)
  • Larry L.Hillblom Foundation Fellowship Grant (2006)
  • K99/R00 NIH Pathway to Independence Award (2006 – 2011)
  • Burroughs Wellcome Career Award in the Biomedical Sciences (2006 – 2013, discontinued 2010)
  • Searle Scholar Award (2010-2013)
  • Margaret Oakley Dayhoff Award from the Biophysical Society (2015)
  • Blavatnik National Science Finalist (2016)
  • Gibco Emerging Leader Prize from the American Society of Cell Biology (2016)
  • Keith R. Porter Fellow Award for Cell Biology (2017)
  • NINDS Director Award (2019)
  • NIH Director Award for service on the NIH Equity Committee (2019)
  • NINDS Director Award (2020)
  • International Award from the Biochemical Society (2023)
  • NIH Director's Innovation Challenge Award (2022-2024)

Research Interests

Cells depend on the asymmetric distribution of their components for homeostasis, differentiation and movement. In no other cell type is this requirement more critical than in the neuron where complex structures are generated during process growth and elaboration and cargo is transported over distances several thousand times the cell body diameter. Microtubules act both as dynamic structural elements and as tracks for intracellular transport.

Microtubules are mosaic polymers containing multiple tubulin isoforms functionalized with abundant posttranslational modifications that are asymmetrically distributed in neurons. An increasing body of evidence supports the hypothesis that the combinatorial information expressed through tubulin genetic and chemical diversity controls microtubule dynamics, mechanics and interactions with microtubule effectors and thus constitutes a 'tubulin code'. Disruption of tubulin modification levels and patterns leads to cancers, neuropathologies and defective axonal regeneration.

Although discovered over thirty years ago, an understanding of the roles of the genetic and chemical complexity of microtubules has remained elusive.  My laboratory aims to understand (i) the biochemical mechanisms of tubulin modification enzymes and how the complex patterns of tubulin posttranslational modifications observed in cells are generated by these enzyme families  (ii) the effects of tubulin posttranslational modifications on the basic properties of the microtubule polymer: its mechanical properties and dynamics and (iii) the effects of tubulin modifications on the recruitment and function of cellular effectors. We take a multifaceted experimental approach to answer these questions integrating structural biology and classic enzymology with single molecule biophysics, live cell imaging and modeling.

Cell Biology and Biophysics Section Overview

Dr. Antonina Roll-Mecak is the Senior Investigator leading the Cell Biology and Biophysics Section of NINDS. The nervous system is composed of a diverse collection of polarized cells that rely on the microtubule cytoskeleton for their specialized functions. The structural and functional diversity of these cell types is reflected at the molecular level in the diversity of the microtubule building blocks, the tubulin dimers. Microtubules are composed of multiple tubulin isotypes that are modified with abundant and chemically diverse posttranslational modifications. Although microtubules were long thought of as inert transport tracks, recent discoveries from our lab and others, reveal that they are information-rich and that their isoform diversity and plethora of posttranslational modifications regulate traffic, microtubule dynamics and mechanics. This “tubulin code” supports the diverse morphology and dynamics of microtubule arrays across cell types, cell cycle and developmental stages. Perturbations in the tubulin code are a hallmark of neurodegeneration and cancers and tubulin modification enzymes are essential for normal development. Despite knowledge of the genetic and chemical complexity of tubulin and its importance to cell physiology dating back to the 1970s, our understanding of its role in microtubule functions is still in its infancy, due in large part to a lack of tools to study the tubulin code. The Roll-Mecak laboratory has pioneered biochemical and biophysical methods for the in vitro reconstitution of the tubulin code and integrates these with structural, proteomic, microscopy-based approaches and modeling to elucidate how the tubulin code regulates microtubule function in health and disease at scales ranging from interactions between single atoms in proteins to the behavior of cells. Many anticancer therapeutics used widely in the clinic target microtubules directly. Our work aims to elucidate the functions of the tubulin code in cell physiology, and also leverages this knowledge for the identification of new targets and approaches for therapeutic intervention.

Lab Members

  • Jiayi Chen, Ph.D., Postdoctoral Fellow
  • Steven Cummings
  • Beth Daley, Ph.D., Postdoctoral Fellow
  • Kishore Mahalingan, Ph.D.
  • Stephanie Sarbanes,  Ph.D., NIGMS PRAT Postdoctoral Fellow
  • Jeffrey Spector, Ph.D.
  • Ewa Szczesna, Ph.D.
  • Agnieszka Szyk, Ph.D.
  • Elena Zehr, Ph.D.
  • Ilia Zhernov, Ph.D.,  Postdoctoral Fellow

Join Our Lab

Our group encompasses biochemists, structural biologists, chemists, microscopists, physicists, and cell biologists. The necessary ingredients are enthusiasm, love of science, rigor and playing well with others.

Graduate Students

Interested in performing your Ph.D. thesis research at the NIH?  We have graduate program partnerships with Johns Hopkins, Brown, Oxford and Cambridge Universities.

For more information visit: The Office of Intramural Training & Education.

Please email Antonina Roll-Mecak if you are a current graduate student interested in applying for a rotation in the Roll-Mecak lab.

Postdoctoral Fellows

The general areas of interest for postdoctoral fellows are:

  • Structural Biology
  • Biochemistry
  • Imaging and Biophysics
  • Cell Biology

Those interested in postdoctoral positions, should send:

  • Cover Letter
  • CV
  • Summary of Research
  • Names of three referees

Postbaccalaureate Fellows

Recent college graduates interested in applying for postbaccalaureate fellowships in the lab, should email Antonina Roll-Mecak and visit the NIH Postbac IRTA website

Undergraduates interested in doing independent study projects or other research opportunities should contact Antonina Roll-Mecak. Please visit  Summer Internship Program (SIP) and NINDS Intramural Training Programs for more information.

Lab News

2024

  • Jiayi's paper on the structure of the tubulin code eraser CCP5 is out in Nature. The study uses cryo-EM, X-ray crystallography, NMR and functional assays to show how CCP5 deforms its substrate to recognize and remove monoglutamate branches from different tubulin isotypes.  Congrats Jiayi, Elena and Aga and special thanks to our collaborators in the Tanner and Tjandra lab!
  • Joe Cleary was awarded a PRAT fellowship from NIGMS. Congrats Joe!!!!
  • Stella Whittaker, our awesome postbac, presents her work on axonal transport at the Annual NIH Research Festival. It is her first poster presentation and she hit it out of the ball park!
  • Kishore's paper on the structural basis of a-tubulin glutamylation by TTLL enzymes is out at Nature Chemical Biology. TTLL6 is not only a writer, but also a reader of the tubulin code, indicating that there is a tubulin code syntax. Congratulations!!!

2023

  • Antonina receives the 2023 International Award from the Biochemical Society at the Dynamic Cell BCSB meeting in the UK
  • Stephanie is awarded a Fellows Award for Research Excellence. Congrats!!! 

2022

2021

  • Kishore is awarded a Fellows Award for Research Excellence. Congrats Kishore!!!
  • Jiayi's microtubule comets design is pictured on the cover of Developmental Cell.
  • Cells have microtubules populations with distinct dynamics. How does this asymmetry arise? Check our recent paper in which we show that tyrosination specific recruitment of regulators at the microtubule ends regulates microtubule dynamics creating microtubule populations with distinct dynamics in cells. Massively fun collaboration with Nikita Gudimchuk and his team on molecular dynamics. Check it out, as well as the nice Preview. Congratulations Jiayi and Aga!
  • Our paper on the mechanism of poly-Glu chain initiation and elongation is out in Nature Structure and Molecular Biology! Fantastic collaboration with Nico Tjandra’s lab at NHLBI and Martin Tanner’s lab at UBC with expert mass spec help from our own Yan Li! C. From inhibitors to structure to enzymatic mechanism. Congrats Kishore, Keith, Maddie and Yanjie!

2020

  • Kishore's paper with the Reber Lab is out in Current Biology!
  • Jiayi was awarded an NINDS postdoctoral fellowship. Congrats Jiayi!
  • Our paper on the cryo-EM structure of katanin bound to the tubulin tail is out in Dev. Cell! Congratulations Elena, Ewa and Aga!

2019

  • Annie gave a great talk on lattice tubulin exchange by severing enzymes at Biophysics.

2018

  • Our paper showing that microtubule severing enzymes promote tubulin exchange within the microtubule is out in Science! Congratulations to Annie, Ewa, Elena and Jeff!

2017

  • Antonina was selected as the 2017 Keith R. Porter fellow! Honored and excited to receive the award from Erika Holzbaur at ASCB. Looking forward to thinking about ways to draw the public and students into the beautiful world of cell biology!
  • Elena gave a great talk on the katanin structure at ASCB!
  • Antonina is promoted to Senior Investigator!
  • Our paper on the structure of katanin using cryo-EM, X-ray diffraction and SAXS is out in Nature Structure and Molecular Biology. More than 25 years after its discovery by Ron Vale, we can now have a first glimpse at this formidable molecular machine. Congratulations Elena and Aga!
  • Farewell party for Keith with the traditional Daruma gift from Antonina. We will miss you Keith and look forward to seeing you paint in the second eye!
  • Our paper on the structure of the TTLL3 tubulin glycylase and the competition between glutamylases and glycylases in estabilishing the tubulin code is out in PNAS. Congratulations Chris, Ian and Yan!
  • JCB profile on what makes Antonina tick, Decoding the secrets of tubulin complexity.
  • Keith was accepted into awesome graduate programs and will start at Duke this fall. Congratulations Keith!
  • Annie was awarded the best poster prize at the Hopkins graduate retreat for her work characterizing the effects of tubulin isoforms on microutbule structure and dynamics. Congratulations Annie!
  • Raj was accepted by all colleges he applied to. Congrats Raj! Well done! He will start at Harvard this coming fall.
  • Annie gave an awesome talk on how tubulin isoforms tune microtubule dynamics to a packed room at ASCB!
  • Raj's research project in our lab for the last two summers earned him a semifinalist position in the Math, Science and Technology Siemens competition and the Regeneron Science Talent Search. Way to go Raj!

2016

  • Chris got one of the two jobs he applied for and will start his own lab the coming fall. Congratulations Chris!
  • Antonina attends the Blavatnik National Awards Gala at the National History Museum in New York. Check out the pictures!
  • Raj won the Outstanding Summer Student Award at NINDS. Congratulations Raj!
  • Antonina won the Emerging Leader Prize from the American Society for Cell Biology. Read the press release from ASCB.
  • Antonina is one of the ten Blavatnik Awards finalists in the Life Sciences! Read the press release from the New York Academy of Sciences and the Blavatnik Foundation.
  • Our paper connecting RPGR glutamylation by TTLL5 to retinal dystrophy is out in PNAS! Congratulations James and thanks to our collaborators in the Li lab!
  • Our paper on the structure and dynamics of recombinant neuronal human microtubules was selected as Paper of the Week by JBC! Congratulations Annie and Jeff and thanks to our collaborator Joe Atherton in Carolyn Moores' lab!
  • Our paper on the rheostatic regulation of microtubule severing by tubulin glutamylation is out in Cell with a nice preview. Congratulations Max!

2015

  • Antonina was selected as one of the Gibco Emerging Leader award finalists by ASCB. Find out more about how she got interesed in science from her ASCB Newsletter essay.
  • Chris was awarded the prize for the best poster at the NINDS retreat describing his work on the structure and mechanism of the TTLL7 glutamylase. Congratulations Chris!
  • Our paper on the mechanism of the TTLL7 glutamylase is out in Cell with a nice preview. Read the press release! Congratulations Chris, Annie and Liz!

2014

  • Antonina is the recipient of the 2015 Margaret Dayhoff Award from the Biophysical Society.
  • Annie is off to start her Ph.D. in the Hopkins-NIH graduate program. We miss you Annie already, but we look forward to having you back soon!
  • Max is off to start in the M.D./Ph.D. program at Harvard. We will miss you Max!
  • Our paper on the tubulin acetyltransferase is out in Cell with a nice preview. Read the press release!
  • Antonina gives a talk at the Porter Neuroscience Center Innaugural Symposium.
  • Annie decides to join the NIH-Hopkins graduate program and continue her exciting work on tubulin modifications in our lab.  We are thrilled that you decided to stay Annie!!!
  • Max is accepted into awesome MD/Ph.D. programs at UCSF, University of Washington, Harvard, Hopkins and Yale.  Maybe I left a few out … Congratulations Max!!!
  • Annie is accepted into awesome graduate programs at Berkeley, UCSF, Hopkins! I might have forgotten a few … Congratulations Annie!!!
  • Porter Neuroscience Research Center dedication and opening.

2012

  • Chris was awarded a Canada Research Council postdoctoral fellowship. Congratulations Chris!
  • Chris was awarded an NINDS postdoctoral fellowship. Congratulations Chris!
  • Antonina teaches in the Physiology course at MBL Woods Hole. Check out the 4th of July microtubule float the students made for that year!

2011

  • The first research paper from the lab is on the cover of Nature Structure and Molecular Biology!
  • The first joint Roll-Mecak and Shroff lab retreat in Tuckahoe State Park
  • We finally move into our space in the Porter Neuroscience Center! Time for a party!
  • Antonina teaches in the Physiology course at MBL Woods Hole.

2010

Publications

2022-2024

Chen, J., Zehr, E.A., Gruschus, J.M., Szyk, A., Liu, Y., Tanner, M.E., Tjandra, N., Roll-Mecak, A. Tubulin   code eraser CCP5 recognizes branch glutamates through substrate deformation. 2024. Nature. 631(8022):905-912. [abstract].

Cummings, S.W., Li, Y., Spector, J.O., Kim, C. and Roll-Mecak, A. The TTLL10 polyglycylase is stimulated by tubulin glutamylation and inhibited by polyglycylation. 2024. eLife . [abstract].

Mahalingan, K.K., Grotjahn, D, Li, Y., Lander, G.C., Zehr, E.A. and Roll-Mecak, A. Structural basis for a-tubulin specific and modification state-depended glutamylation. 2024. Nature Chem. Biol. In press. [abstract].

McKenna, E.D., Sarbanes, S.L., Cummings, S.W., Roll-Mecak, A. The tubulin code, from molecules to health and disease. 2023. Annu. Rev. Cell. Dev. 39:331-361. [abstract].

Chen, J. and Roll-Mecak, A. Glutamylation is a negative regulator of microtubule growth. 2023. Mol. Biol. Cell. 34(7):ar70 1-13. [abstract].

Szczesna, E., Zehr, E.A., Cummings, S.W., Szyk, A., Mahalingan, K.K., Li Y., Roll-Mecak, A. Combinatorial and antagonistic effects of tubulin glutamylation and glycylation on katanin microtubule severing. 2022. Dev. Cell. 57(21):2497-2513. [abstract].

Sarbanes S.L., Zehr, E.A., Roll-Mecak, A. Microtubule-severing enzymes. 2022. Curr. Biol. 32(19):R992-R997. [abstract].

Zehr, E.A., Roll-Mecak, A. A look under the hood of the machine that makes cilia beat. 2022. Nature Struct. & Molec. Biol. 29(5):416-418. [abstract].

Zhuang, Z.,Cummings, S.W., Roll-Mecak, A., Tanner, M.E. Phosphinic acid-based inhibitors of tubulin polyglycylation. 2022. Chem. Commun. (Camb.) 58(45):6530-6533. [abstract].

Zheng, P., Obara, C.J., Szczesna, E., Nixon-Abell, J., Mahalingan, K.K., Roll-Mecak, A., Lippincott-Schwartz, J., Blackstone, C. ER proteins decipher the tubulin code to regulate organelle distribution. 2022. Nature 601(7891):132-138. [abstract].

2019-2021

Chen, J., Kholina, E., Szyk, A., Fedorov, V.A., Kovalenko, I., Gudimchuk, N., Roll-Mecak, A. α-tubulin tail modifications regulate microtubule stability through selective effector recruitment, not changes in intrinsic polymer dynamics. 2021. Dev. Cell. 56(14):2016-2028. [abstract] [cover]

Commentary by Mani and Subramanian in Dev. Cell. 56(14): 2007-2009.

Bradke, F., Roll-Mecak, A. Editorial overview: Microtubules in nervous system development. 2020. Dev. Nerurobiol. 81(3):229-230.

Mahalingan, K.K., Keith Keenan, E., Strickland, M., Li, Y., Liu, Y., Ball, H.L., Tanner, M.E., Tjandra, N., Roll-Mecak, A. Structural basis for polyglutamate chain initiation and elongation by TTLL family enzymes. 2020. Nature Struct. & Molec. Biol. 27(9):802-813. [abstract]

Gudimchuk, N.B., Ulyanov, E.V., O'Toole, E., Page, C.L., Vinogradov, D.S., Morgan, G., Li, G., Moore, J.K., Szczesna, E., Roll-Mecak, A., Ataullakhanov, F.I., Richard McIntosh, J. Mechanisms of microtubule dynamics and force generation examined with computational modeling and electron cryotomography. 2020.  Nature Commun. 11(1):3765. [abstract]

Roll-Mecak, A. The Tubulin Code in Microtubule Dynamics and Information Encoding. 2020. Dev. Cell. 54(1):7-20. [abstract]

Vemu, A., Szczesna E. and Roll-Mecak, A. In Vitro Reconstituiton Assays of Microtubule Amplification and Lattice Repair by the Microtubule-Severing Enzymes Katanin and Spastin. 2020. Methods Mol Biol. 2101:27-38. [abstract]

Spector, J.O, Vemu, A. and Roll-Mecak, A. In Vitro Microtubule Dynamics Assays Using Dark-Field Microscopy. 2020. Methods Mol Biol. 2101:39-51. [abstract] 

Atherton, J., Luo, Y., Xiang, S., Yang, C., Rai, A., Jiang, K., Stangier, M., Vemu, A., Cook, A.D., Wang, S., Roll-Mecak, A., Steinmetz, M.O., Akhmanova, A., Baldus, M., Moores, C.A. Structural determinants of microtubule minus end preference in CAMSAP CKK domains. 2019. Nature Commun. 10(1):5326. [abstract]

Zehr, E.A., Szyk, A., Szczesna, E., Roll-Mecak, A. Katanin Grips the β-Tubulin Tail Through an Electropositive Double Spiral to Sever Microtubules. 2020. Dev. Cell. 52(1):118-131. [abstract] 

Editor’s choice Science 357(6354):883-884.

Roll-Mecak, A. A microtubule-myelination connection. 2019. Cell. 179(1):54-46.[abstract]

Sandate, C., Szyk, A., Zehr, E.A., Lander, G.C. and Roll-Mecak, A. An allosteric network in spastin couples multiple activities required for microtubule severing. 2019. Nature Struct. & Molec. Biol. 26(8):671-678.[abstract]

Gudimchuk, N. and Roll-Mecak, A. Watching microtubules grow one tubulin at a time. 2019. Proc. Natl. Acad. Sci. 116(15):7163-7165.[abstract]

Roll-Mecak, A. How cells exploit tubulin diversity to build functional cellular microtubule mosaics. 2019. Curr. Opin. Cell Biol. 56:102-108.[abstract]

2016-2018

McNally, F. and Roll-Mecak, A. Microtubule severing enzymes: from cellular functions to molecular mechanism. 2018. J. Cell Biol. 217(12):4057-4069.[abstract]

Vemu, A., Szczesna, E., Zehr, E.A., Spector, J.O., Grigorieff, N.G., Deaconescu, A.M.and Roll-Mecak, A. Severing enzymes amplify microtubule arrays through lattice GTP-tubulin incorporation. 2018. Science 361:6404.[abstract]

Commentary by Stavoe and Holzbaur in Dev. Cell 47(4):402-403.

Commentary by Akhmanova in Dev. Cell 47(4):400-401.                                                                             

Park, J. and Roll-Mecak, A. The tubulin code in neuronal polarity. 2018. Curr. Opinion Neurobiology 51:95-102.[abstract] 

Vemu, A., Atherton, J., Spector, J.O., Moores, C.M. and Roll-Mecak, A. Tubulin isoform composition tunes microtubule dynamics. 2017. Mol. Biol. Cell. 28(25):3564-3572.[abstract]

Zehr, E., Szyk, A. Szczesna, E, Zuo, X and Roll-Mecak, A. Katanin spiral and ring structures shed light on power stroke for microtubule severing. 2017. Nature Struct. & Molec. Biol. 24(9):717-725. [abstract] 

Garnham, C.P., Yu, I., Li, Y. and Roll-Mecak, A. Crystal structure of Tubulin Tyrosine Ligase-Like 3 reveals essential architectural elements unique to tubulin monoglycylases. 2017. Proc. Natl. Acad. Sci. USA. 114(25):6545-6550. [abstract]

Pigino, G. and Roll-Mecak, A. Microtubule dynamics: 50 years after the discovery of tubulin and still going strong. 2017. Mol. Biol. Cell. 28(6):705-706. [abstract]

Sun, X., Park, J.H., Gumerson, J., Wu, Z., Swaroop, A., Qian, H., Roll-Mecak, A. and Li, T. Loss of RPGR glutamylation underlies the pathogenic mechanism of retinal dystrophy caused by TTLL5 mutations. 2016. Proc. Natl. Acad. Sci. USA.,13(21): :E2925-2934. [abstract]

Vemu, A., Atherton, J., Spector, J.O., Szyk, A., Moores, C.M. and Roll-Mecak, A. Structure and Dynamics of Single-Isoform Recombinant Neuronal Human Tubulin. 2016. J. Biol. Chem. Accelerated Communication, 291(25):12907-12915. [abstract]

Meyer, P.A., Socias, S., Key. J., Ransey, E., Tjon, E.C., Buschiazzo, A., Lei, M., Botka, C., Withrow, J., Neau, D., Rajashankar, K., Anderson, K.S., Baxter, R.H., Blacklow, S.C., Boggon, T.J., Bonvin, A.M., Borek, D., Brett, T.J., Caflisch, A., Chang, C.I., Chazin, W.J., Corbett, K.D., Cosgrove, M.S., Crosson, S., Dhe-Paganon, S., Di Cera, E., Drennan, C.L., Eck, M.J., Eichman, B.F., Fan, Q.R., Ferré-D'Amaré, A.R., Christopher Fromme, J., Garcia, K.C., Gaudet, R., Gong, P., Harrison ,S.C., Heldwein, E.E., Jia, Z., Keenan, R.J., Kruse, A.C., Kvansakul ,M., McLellan, J.S., Modis, Y., Nam, Y., Otwinowski, Z., Pai, E.F., Pereira, P.J., Petosa, C., Raman, C.S., Rapoport, T.A., Roll-Mecak, A,. Rosen, M.K., Rudenko, G., Schlessinger, J., Schwartz, T.U., Shamoo, Y., Sondermann, H., Tao, Y.J., Tolia, N.H., Tsodikov, O.V., Westover, K.D., Wu, H., Foster, I., Fraser, J.S., Maia, F.R., Gonen, T., Kirchhausen, T., Diederichs, K., Crosas, M., Sliz, P. Data publication with the structural biology data grid supports live analysis. 2016. Nature Commun. 7:10882. doi: 10.1038/ncomms10882. [abstract]

26. Valenstein, M.L. and Roll-Mecak, A. Graded control of microtubule severing by tubulin glutamylation. 2016. Cell. 164(5): 911-921. [abstract]

Commentary by Schaletzky and Rape in Cell 164(5): 836-837.

2013-2015

Garnham, C.P., Vemu, A., Wilson-Kubalek, E.M., Yu, I., Szyk, A., Lander, G.C., Milligan, R.A. Roll-Mecak, A. Multivalent microtubule recognition by tubulin tyrosine ligase-like family glutamylases. 2015. Cell. 161(5):1112-1123. [abstract]

Commentary by Raunser and Gatsogiannis in Cell 151(5): 960-961.

Yu, I., Garnham, C.P. and Roll-Mecak, A. Writing and Reading the Tubulin Code. 2015. J. Biol. Chem. 290(28): 17163-17172 “The State of the Cytoskeleton in 2015” special issue [abstract]

Roll-Mecak, A. Intrinsically disordered tubulin tail: complex tuners of microtubule functions? 2014. Seminars Cell. Dev. Biol. 37: 11-19. [abstract]

Szyk, A., Deaconescu, A. M., Spector, J., Goodman, B. J., Valenstein, M. V., Ziolkowska, N. E., Kormendi, V., Grigorieff, N., Roll-Mecak, A. Molecular basis of age dependent microtubule acetylation. 2014. Cell. 157(6): 1405-1415. [abstract]

Commentary by Kull and Sloboda in Cell, ACS Chemical Biology, Eureka Alert and Nanowerk.

Vemu, A., Garnham, C. P., Lee, D.Y., Roll-Mecak, A. Generation of differentially modified microtubules using in vitro enzymatic approaches. 2014. Methods in Enzymology. 540: 149-166. [abstract]

Roll-Mecak, A. (2013). Shining light at microtubule crossroads. Science 342(6163):1180-1181. [abstract]

Ziolkowska, N. and Roll-Mecak, A. In vitro microtubule severing assays. 2013. Methods in Molecular Biology. 1046: 323-334. [abstract] 

Szyk, A., Piszczek, G. and Roll-Mecak, A. Tubulin tyrosine ligase and stathmin compete for tubulin binding in vitro. 2013. J. Mol. Biol. 425(14): 2412-2414. [abstract] 

Liu, Y., Garnham, C.P., Roll-Mecak, A. and Tanner, M.E. Phosphinic Acid-Based Inhibitors of Tubulin Polyglutamylases. 2013. Bioorg. Med. Chem. Lett. 23(15): 4408-4412. [abstract] 

2010-2012

Garnham, C. P. and Roll-Mecak, A. The chemical complexity of cellular microtubules: Tubulin post-translational modification enzymes and their roles in tuning microtubule functions. 2012. Cytoskeleton. 69(7): 442-463. [abstract]

Kormendi, V., Szyk, A., Piszczek, G., Roll-Mecak, A. Crystal structures of tubulin acetyltransferase reveal a conserved catalytic core and the plasticity of the essential N-terminus. 2012. J. Biol. Chem. 287(50): 41569-41575. [abstract]

Szyk, A., Deaconescu, A.M., Piszczek, G., Roll-Mecak, A. Tubulin tyrosine structure reveals adaptation of an ancient fold to bind and modify tubulin. 2011. Nature Struct. & Molec. Biol. 8(11): 1250-1258. [cover] [abstract] 

Roll-Mecak, A. and McNally, F.J. Microtubule severing enzymes, 2010. Curr. Opin. Cell Biol., 22(1): 96-103. [abstract]

A. Roll-Mecak Publications 1999-2009

Roll-Mecak, A. and Vale, R.D. Structural basis for microtubule severing by the hereditary spastic paraplegia protein spastin. 2008. Nature, 451(7176): 363-367. [abstract] 

Roll-Mecak, A. and Vale, R.D. Making more microtubules by severing: a common theme of noncentrosomal microtubule arrays? 2006. J. Cell. Biol. 175 (6): 849-851. [abstract]

Padyana, A. K., Qiu, H., Roll-Mecak, A., Hinnebusch, A. G., Burley, S. K. Structural basis for autoinhibition and mutational activation of eIF2a protein kinase GCN2. 2005. J. Biol. Chem. 280(32): 29289-29299. [abstract] 

Roll-Mecak, A. and Vale, R. D. The Drosophila Homologue of the Hereditary Spastic Paraplegia Protein, Spastin, Severs and Disassembles Microtubules. 2005. Curr. Biol. 5(7): 650-655. [abstract]

Roll-Mecak, A., Alone, P., Cao, C., Dever, T. E., and Burley, S. K. X-ray structure of translation initiation factor eIF2g: implications for tRNA and eIF2a binding. 2004. J. Biol. Chem. 279(11): 10634-10642. [abstract]

Shin, B-S., Maag, D., Roll-Mecak, A., Arefin, S.M., Burley, S.K., Lorsch, J.R., and Dever, T.E. Uncoupling the GTPase and Translational Activity of Initiation Factor eIF5B/IF2 by Mutations that Lower Ribosome Affinity. 2003. Cell 111: 1015-1025. [abstract]

Deaconescu, A.M., Roll-Mecak, A., Bonanno, J.B., Gerchman, S. E., Kycia, H., William, B.F., and Burley, S.K.  X-ray Structure of Saccharomyces Mitochondrial Matrix Factor 1 (Hmf1). 2002. Proteins 42(2): 431-436. [abstract]

Roll-Mecak, A., Shin, B-S, Dever, T.E., and Burley, S.K. Engaging the ribosome: Universal IFs of translation. 2001. Trends Biochem. Sci. 26(12): 705-709. [abstract]

Dever, T.E., Roll-Mecak, A., Choi, S.K., Lee, J.H., Cao, C., Shin, B-S., and Burley, S.K. The Universal Translation Initiation Factor IF2/eIF5B. 2001. Cold Spring Harbor Symp. Quant. Biol. 66: 417-424.

Roll-Mecak, A., Cao, C., Dever, T.E., and Burley, S.K. X-ray structures of the Universal Translation Initiation Factor IF2/eIF5B: Conformational Changes on GDP and GTP Binding. 2000. Cell 103 (5): 781-792. [abstract]

Choi, S. K., Olsen, D.S., Roll-Mecak, A., Martung, A., Remo, K. L., Burley, S. K., Hinnebusch, A. G., and Dever, T. E.  Physical and functional interaction between the eukaryotic orthologs of prokaryotic translation initiation factors IF1 and IF2. 2000. Mol. Cell. Biol. 20: 7183-7191. [abstract]

Lee, J.H., Choi, S.K., Roll-Mecak, A., Burley, S. K., and Dever, T. E.  Universal conservation in translation initiation revealed by human and archaeal homologs of bacterial translation initiation factor IF2.1999. Proc. Natl. Acad. Sci. USA. 96: 4342-4347. [abstract] 

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