Direct and indirect effects of tubulin post-translational modifications on microtubule stability: Insights and regulations

被引:23
作者
Baer, Julia
Popp, Yannes
Bucher, Michael
Mikhaylova, Marina
机构
[1] Humboldt Univ, Inst Biol, RG Optobiol, Invalidenstr 42, D-10115 Berlin, Germany
[2] Univ Med Ctr Hamburg Eppendorf, Guest Grp Neuronal Prot Transport, Ctr Mol Neurobiol, ZMNH, Falkenried 94, D-20251 Hamburg, Germany
来源
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH | 2022年 / 1869卷 / 06期
关键词
Microtubules; Detyrosination; Acetylation; aTAT1; VASH; Calpain; DEPENDENT PROTEIN-KINASE; ALPHA-BETA-TUBULIN; TYROSINE-LIGASE; M-CALPAIN; STRUCTURAL INSIGHTS; CRYSTAL-STRUCTURE; ACETYLATION; HDAC6; SIRT2; ACETYLTRANSFERASE;
D O I
10.1016/j.bbamcr.2022.119241
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Microtubules (MTs) mediate various cellular functions such as structural support, chromosome segregation, and intracellular transport. To achieve this, the pivotal properties of MTs have to be changeable and tightly controlled. This is enabled by a high variety of tubulin posttranslational modifications, which influence MT properties directly, via altering the MT lattice structurally, or indirectly by changing MT interaction partners. Here, the distinction between these direct and indirect effects of MT PTMs are exemplified by acetylation of the luminal alpha-tubulin K40 resulting in decreased rigidity of MTs, and by MT detyrosination which decreases inter-action with depolymerizing proteins, thus causing more stable MTs. We discuss how these PTMs are reversed and regulated, e.g. on the level of enzyme transcription, localization, and activity via various signalling pathways including the conventional calcium-dependent proteases calpains and how advances in microscopy techniques and development of live-sensors facilitate the understanding of MT PTM interaction and effects.
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页数:11
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