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Title page for ETD etd-09232003-180406


Type of Document Dissertation
Author Carnahan Jr., Robert Herschel
Author's Email Address robert.carnahan@vanderbilt.edu
URN etd-09232003-180406
Title The PCH family protein, Cdc15p, interacts directly with two actin nucleation pathways to contribute to cytokinetic actin ring formation in schizosaccharomyces pombe
Degree PhD
Department Cell and Developmental Biology
Advisory Committee
Advisor Name Title
Gary Olson Committee Chair
Carl Johnson Committee Member
David Greenstein Committee Member
Kathleen L. Gould Committee Member
Todd Graham Committee Member
Keywords
  • Medial Ring
  • Cytokinesis
  • Mitosis
Date of Defense 2003-08-06
Availability unrestricted
Abstract
Cytokinetic actomyosin ring formation (CAR) in S. pombe requires two independent actin nucleation pathways, one dependent on the Arp2/3 complex and another involving the formin Cdc12p. Here we investigate the role of the PCH family protein, Cdc15p, in CAR assembly and find that it interacts with proteins from both of these nucleation pathways. Cdc15p binds directly to the Arp2/3 complex activator Myo1p, which likely explains why actin patches and the Arp2/3 complex fail to be medially recruited during mitosis in cdc15 mutants. Cdc15p also binds directly to Cdc12p. Cdc15p and Cdc12p not only display mutual dependence for CAR localization, but also exist together in a ring nucleating structure prior to CAR formation. The disruption of these interactions in cdc15 null cells is likely to be the reason for their complete lack of CARs. We propose a model in which Cdc15p plays a critical role in recruiting and coordinating the pathways essential for the assembly of medially located F-actin filaments and construction of the CAR.
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