HKUST Library Institutional Repository Banner

HKUST Institutional Repository >
Division of Life Science >
LIFS Master Theses  >

Please use this identifier to cite or link to this item: http://hdl.handle.net/1783.1/7577
Title: Identification and characterization of various populations of the [gamma]-tubulin ring complex
Authors: Shen, Yuehong
Issue Date: 2012
Abstract: The microtubule (MT) network is a major component of the cellular cytoskeleton. Its importance towards cellular function is reflected in its roles in cell proliferation, intracellular transport, and cell migration. A crucial element of MT organization is the γ-tubulin ring complex (γTuRC). This evolutionarily conserved entity is responsible for microtubule nucleation at the centrosomes, near the mitotic chromatin, and also within existing spindle microtubules. The γTuRC also acts as a stability factor for microtubules by virtue of its MT-minus end capping function, thereby preventing depolymerization. It is well known that the γTuRC contains members of a conserved protein family called GCPs. Recently several novel γTuRC-binding proteins are identified, such as CDK5RAP2, GCP-WD and MOZART1. However, despite the elucidation of key roles for these proteins in centrosomal attachment, MT nucleation, and mitotic spindle organization, it remains unclear how their roles are integrated in the regulation of the γTuRC. In our present studies, we have uncovered that despite their direct binding to the γTuRC, CDK5RAP2, GCP-WD and MOZART1 exist in different γTuRC populations, and they also have distinct γTuRC binding preferences in different stages of cell cycle. Our data suggests that CDK5RAP2, GCP-WD and MOZART1 may be under distinct control for interacting with the γTuRC.
Description: Thesis (M.Phil.)--Hong Kong University of Science and Technology, 2012
xi, 41 p. : ill. (some col.) ; 30 cm
HKUST Call Number: Thesis LIFS 2012 Shen
URI: http://hdl.handle.net/1783.1/7577
Appears in Collections:LIFS Master Theses

Files in This Item:

File Description SizeFormat
th_redirect.html0KbHTMLView/Open

All items in this Repository are protected by copyright, with all rights reserved.