Mechanisms for concentrating Rho1 during cytokinesis

Satoshi Yoshida, Sara Bartolini, David Pellman

Research output: Contribution to journalArticle

84 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)810-823
Number of pages14
JournalGenes and Development
Volume23
Issue number7
DOIs
Publication statusPublished - 2009 Apr 1

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Keywords

  • Cytokinesis
  • GEF
  • Polybasic sequence
  • Rho1
  • Yeast

ASJC Scopus subject areas

  • Genetics
  • Developmental Biology

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