National Library of Medicine

54. 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. Cell57(21):2497-2513. [abstract] [pdf(pdf, 4766 KB)].

53. Sarbanes S.L., Zehr, E.A., Roll-Mecak, A. Microtubule-severing enzymes. 2022. Curr. Biol. 32(19):R992-R997. [abstract] [pdf(pdf, 2083 KB)].

52. 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] [pdf(pdf, 1091 KB)].

51. 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] [pdf(pdf, 1692 KB)]

50. 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] [pdf(pdf, 3527 KB)]


49. 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] [pdf(pdf, 3499 KB)]

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

48. Bradke, F., Roll-Mecak, A. Editorial overview: Microtubules in nervous system development. 2020. Dev. Nerurobiol. 81(3):229-230. [pdf(pdf, 57 KB)]

47. 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] [pdf(pdf, 2474 KB)]

46. 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] [pdf(pdf, 3315 KB)]

45. Roll-Mecak, A. The Tubulin Code in Microtubule Dynamics and Information Encoding. 2020. Dev. Cell. 54(1):7-20. [abstract] [pdf(pdf, 3120 KB)]

44. 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] [pdf(pdf, 1174 KB)]

43. 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] [pdf(pdf, 1161 KB)]

42. 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] [pdf(pdf, 7759 KB)]

41. 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] [pdf(pdf, 5806 KB)]

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

40. Roll-Mecak, A. A microtubule-myelination connection. 2019. Cell. 179(1):54-46.[abstract] [pdf(pdf, 728 KB)]

39. 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] [pdf(pdf, 4498 KB)]

38. Gudimchuk, N. and Roll-Mecak, A. Watching microtubules grow one tubulin at a time. 2019. Proc. Natl. Acad. Sci. 116(15):7163-7165.[abstract] [pdf(pdf, 720 KB)]

37. Roll-Mecak, A. How cells exploit tubulin diversity to build functional cellular microtubule mosaics. 2019. Curr. Opin. Cell Biol. 56:102-108.[abstract] [pdf(pdf, 1334 KB)]


36. McNally, F. and Roll-Mecak, A. Microtubule severing enzymes: from cellular functions to molecular mechanism. 2018. J. Cell Biol. 217(12):4057-4069.[abstract] [pdf(pdf, 1922 KB)]

35. 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] [pdf(pdf, 9179 KB)]

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

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

34. Park, J. and Roll-Mecak, A. The tubulin code in neuronal polarity. 2018. Curr. Opinion Neurobiology 51:95-102.[abstract] [pdf(pdf, 843 KB)]

33. 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] [pdf(pdf, 1301 KB)]

32. 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] [pdf(pdf, 3320 KB)]

31. 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] [pdf(pdf, 1900 KB)]

30. 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] [pdf(pdf, 58 KB)]

29. 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] [pdf(pdf, 2225 KB)]

28. 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] [pdf(pdf, 2968 KB)]

27. 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] [pdf(pdf, 1901 KB)]

26. Valenstein, M.L. and Roll-Mecak, A. Graded control of microtubule severing by tubulin glutamylation. 2016. Cell. 164(5): 911-921. [abstract] [pdf(pdf, 2612 KB)]

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


25. 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] [pdf(pdf, 4842 KB)]

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

24. 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] [pdf(pdf, 1810 KB)]

23. Roll-Mecak, A. Intrinsically disordered tubulin tail: complex tuners of microtubule functions? 2014. Seminars Cell. Dev. Biol. 37: 11-19. [abstract] [pdf(pdf, 1928 KB)]

22. 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] [pdf(pdf, 2524 KB)]

Commentary by Kull and Sloboda in CellACS Chemical BiologyEureka Alert and Nanowerk.

21. 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] [pdf(pdf, 1175 KB)]

20. Roll-Mecak, A. (2013). Shining light at microtubule crossroads. Science 342(6163):1180-1181. [abstract] [pdf(pdf, 429 KB)]

19. Ziolkowska, N. and Roll-Mecak, A. In vitro microtubule severing assays. 2013. Methods in Molecular Biology. 1046: 323-334. [abstract] [pdf(pdf, 263 KB)]

18. 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] [pdf(pdf, 542 KB)]

17. 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] [pdf(pdf, 891 KB)]


16. 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] [pdf(pdf, 1795 KB)]

15. 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] [pdf(pdf, 1643 KB)]

14. 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] [pdf(pdf, 2748 KB)]

13. Roll-Mecak, A. and McNally, F.J. Microtubule severing enzymes, 2010. Curr. Opin. Cell Biol., 22(1): 96-103. [abstract] [pdf(pdf, 382 KB)]

A. Roll-Mecak Publications 1999-2009

12. 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] [pdf(pdf, 1868 KB)]

11. 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] [pdf(pdf, 742 KB)]

10. 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] [pdf(pdf, 2948 KB)]

9. 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] [pdf(pdf, 508 KB)]

8. 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 binding2004. J. Biol. Chem. 279(11): 10634-10642. [abstract] [pdf(pdf, 1711 KB)]

7. 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] [pdf(pdf, 458 KB)]

6. 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] [pdf(pdf, 1425 KB)]

5. 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] [pdf(pdf, 141 KB)]

4. 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. [pdf(pdf, 231 KB)]

3. 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] [pdf(pdf, 1842 KB)]

2. 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] [pdf(pdf, 735 KB)]

1. 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] [pdf(pdf, 292 KB)]

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