Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/23181
Title: Functional analysis of syp1, a novel substrate of the serine/threonine kinase prk1
Authors: QIU WENJIE
Keywords: actin, septin, Syp1p, Prk1p, cell division, cytokinesis
Issue Date: 30-Oct-2007
Source: QIU WENJIE (2007-10-30). Functional analysis of syp1, a novel substrate of the serine/threonine kinase prk1. ScholarBank@NUS Repository.
Abstract: In budding yeast, the actin and septin cytoskeletons are important for the establishment of cell polarity. During the cell cycle, these cytoskeletons undergo dramatic reorganization which is regulated by many cytoskeleton-associated proteins. In this study, Syp1p has been found to have functional interactions with the actin cytoskeleton. Syp1p is a new substrate of Prk1p, a kinase that regulates actin dynamics. Syp1p colocalizes with actin cytoskeleton whose integrity is required for the polarized localization of Syp1p. Syp1p can physically interact with the actin-associated protein Sla1p. Furthermore, Syp1p overexpression suppresses the defects of BNI1 deletion mutant. In addition to its roles in actin cytoskeleton, Syp1p is also discovered to be a new regulator of the septin dynamics. Syp1p colocalizes and physically interacts with septins. Syp1p overexpression disorganizes septin structure and induces the Swe1p-dependent elongated bud phenotype. Syp1p also regulates the organization of septins in different cell cycle stages.
URI: http://scholarbank.nus.edu.sg/handle/10635/23181
Appears in Collections:Ph.D Theses (Open)

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