Cytokinesis mediated through the recruitment of cortexillins into the cleavage furrow

被引：96

作者：

Weber, I ^{[1
]}

Gerisch, G ^{[1
]}

Heizer, C ^{[1
]}

Murphy, J ^{[1
]}

Badelt, K ^{[1
]}

Stock, A ^{[1
]}

Schwartz, JM ^{[1
]}

Faix, J ^{[1
]}

机构：

[1] Max Planck Inst Biochem, D-82152 Martinsried, Germany

来源：

EMBO JOURNAL | 1999年 / 18卷 / 03期

关键词：

cleavage furrow; cortexillin; cytokinesis; Dictyostelium; protein targeting;

D O I：

10.1093/emboj/18.3.586

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：

The fact that substrate-anchored Dictyostelium cells undergo cytokinesis in the absence of myosin II underscores the importance of other proteins in enabling the cleavage furrow to constrict. Cortexillins, a pair of actin-bundling proteins, are required for normal cleavage. They are targeted to the incipient furrow in wild-type and, more prominently, in myosin II-null cells. No other F-actin bundling or cross-linking protein tested is co-localized, Green fluorescent protein fusions show that the N-terminal actin-binding domain of cortexillin I is dispensable and the C-terminal region is sufficient for translocation to the furrow and the rescue of cytokinesis. Cortexillins are suggested to have a targeting signal for coupling to a myosin II-independent system that directs transport of membrane proteins to the cleavage furrow.

引用

页码：586 / 594

页数：9

共 41 条

[1] Dictyostelium myosin II null mutant can still cap Con A receptors [J].