Binding of alpha-fodrin to gamma-tubulin accounts for its role in the inhibition of microtubule nucleation

被引：4

作者：

Sreeja, Jamuna S. ^{[1
]}

Nellikka, Rohith Kumar ^{[1
]}

John, Rince ^{[1
]}

Sivakumar, Krishnankutty C. ^{[2
]}

Sreekumar, Easwaran ^{[3
]}

Sengupta, Suparna ^{[1
]}

机构：

[1] Rajiv Gandhi Ctr Biotechnol, Canc Res Programme, Trivandrum, Kerala, India

[2] Rajiv Gandhi Ctr Biotechnol, Distributed Informat Sub Ctr, Trivandrum, Kerala, India

[3] Rajiv Gandhi Ctr Biotechnol, Viral Dis Biol, Trivandrum, Kerala, India

来源：

FEBS LETTERS | 2019年 / 593卷 / 11期

关键词：

fodrin; gamma-tubulin; GRIP2; motif; microtubule; nucleation; PROTEIN INTERACTIONS; CELL-CYCLE; COMPLEXES; RING;

D O I：

10.1002/1873-3468.13425

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：

Non-erythroid spectrin or fodrin is present as part of the gamma-tubulin ring complex (gamma-TuRC) in brain tissue and brain derived cells. Here, we show that fodrin, which is otherwise known for providing structural support to the cell membrane, interacts directly with gamma-tubulin within the gamma-TuRC through a GRIP2-like motif. Turbidometric analysis of microtubule polymerization with nucleation-potent gamma-TuRC isolated from HEK-293 cells that lack fodrin and the gamma-TuRC from goat brain that contains fodrin shows inefficiency of the latter to promote nucleation. The involvement of fodrin was confirmed by the reduction in the microtubule polymerization efficiency of HEK-293 derived gamma-TuRCs upon addition of purified brain fodrin. Thus, the interaction of fodrin with gamma-tubulin is responsible for its inhibitory effect on gamma-tubulin mediated microtubule nucleation.

引用

页码：1154 / 1165

页数：12

共 16 条

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