Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/16262
Title: Phosphoregulation of actin-driven endocytosis in the yeast saccharomyces cerevisiae
Authors: HUANG BO
Keywords: actin, endocytosis, phosphorylation, dephosphorylation, Glc7p, Prk1p
Issue Date: 18-Jun-2007
Source: HUANG BO (2007-06-18). Phosphoregulation of actin-driven endocytosis in the yeast saccharomyces cerevisiae. ScholarBank@NUS Repository.
Abstract: Actin is indispensable for the clathrin-mediated endocytosis. Actin polymerization that drives the internalization step is tightly regulated, best studied by the Prk1p kinase. Prk1p phosphorylates endocytic protein Pan1p and ultimately triggers the termination of actin polymerization. In this thesis work the minimal phosphorylation motif of Prk1p was first determined as [L/I/V/M] xxxxTG. Scd5p was then validated as a novel target for Prk1p. This also led to the answer to a major question in the regulatory pathway of actin-driven endocytosis: how Pan1p is relieved from phospho-inhibition. The type I phosphatase Glc7p and its targeting subunit Scd5p were confirmed to be involved in the dephosphorylation process. Two targeting routes for the Glc7p-Scd5p complex to Pan1p were uncovered. First, Scd5p binds Pan1p directly. Second, an indirect route. Scd5p has a high affinity for End3p, a binding partner of Pan1p. Altogether these findings significantly advanced our understanding of the regulatory complexity of endocytosis.
URI: http://scholarbank.nus.edu.sg/handle/10635/16262
Appears in Collections:Ph.D Theses (Open)

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