The Chemical Complexity of Cellular Microtubules: Tubulin Post-Translational Modification Enzymes and Their Roles in Tuning Microtubule Functions

被引：146

作者：

Garnham, Christopher P.

Roll-Mecak, Antonina ^{[1
,2
]}

机构：

[1] NINDS, Cell Biol & Biophys Unit, Porter Neurosci Res Ctr, NIH, Bethesda, MD 20892 USA

[2] NHLBI, Bethesda, MD 20892 USA

来源：

CYTOSKELETON | 2012年 / 69卷 / 07期

关键词：

microtubule; tubulin modifications; TTL; motor; post-translational modifications; NONTYROSINATED ALPHA-TUBULIN; SPASTIC PARAPLEGIA PROTEIN; DYNAMICS IN-VITRO; BETA-TUBULIN; TYROSINE-LIGASE; RAT-BRAIN; DETYROSINATED MICROTUBULES; ENDOPLASMIC-RETICULUM; ACETYLATED TUBULIN; CYTOSOLIC CARBOXYPEPTIDASES;

D O I：

10.1002/cm.21027

中图分类号：

Q2 [细胞生物学];

学科分类号：

071013 [干细胞生物学];

摘要：

Cellular microtubules are marked by abundant and evolutionarily conserved post-translational modifications that have the potential to tune their functions. This review focuses on the astonishing chemical complexity introduced in the tubulin heterodimer at the post-translational level and summarizes the recent advances in identifying the enzymes responsible for these modifications and deciphering the consequences of tubulin's chemical diversity on the function of molecular motors and microtubule associated proteins. Published 2012 Wiley Periodicals, Inc.

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页码：442 / 463

页数：22

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