Mechanisms for concentrating Rho1 during cytokinesis

Satoshi Yoshida, Sara Bartolini, David Pellman*

*この研究の対応する著者

研究成果: Article査読

97 被引用数 (Scopus)

抄録

The small GTP-binding protein, Rho1/RhoA plays a central role in cytokinetic actomyosin ring (CAR) assembly and cytokinesis. Concentration of Rho proteins at the division site is a general feature of cytokinesis, yet the mechanisms for recruiting Rho to the division site for cytokinesis remain poorly understood. We find that budding yeast utilizes two mechanisms to concentrate Rho1 at the division site. During anaphase, the primary mechanism for recruiting Rho1 is binding to its guanine nucleotide exchange factors (GEFs). GEF-dependent recruitment requires that Rho1 has the ability to pass through its GDP or unliganded state prior to being GTP-loaded. We were able to test this model by generating viable yeast lacking all identifiable Rho1 GEFs. Later, during septation and abscission, a second GEF-independent mechanism contributes to Rho1 bud neck targeting. This GEF-independent mechanism requires the Rho1 polybasic sequence that binds to acidic phospholipids, including phosphatidylinositol 4,5-bisphosphate (PIP2). This latter mechanism is functionally important because Rho1 activation or increased cellular levels of PIP2 promote cytokinesis in the absence of a contractile ring. These findings comprehensively define the targeting mechanisms of Rho1 essential for cytokinesis in yeast, and are likely to be relevant to cytokinesis in other organisms.

本文言語English
ページ(範囲)810-823
ページ数14
ジャーナルGenes and Development
23
7
DOI
出版ステータスPublished - 2009 4月 1
外部発表はい

ASJC Scopus subject areas

  • 遺伝学
  • 発生生物学

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