Date of Award
2003
Publication Type
Master Thesis
Degree Name
M.Sc.
Department
Biological Sciences
Keywords
Chemistry, Biochemistry.
Supervisor
Hubberstey, A.
Rights
info:eu-repo/semantics/openAccess
Creative Commons License
This work is licensed under a Creative Commons Attribution-NonCommercial-No Derivative Works 4.0 International License.
Abstract
The actin cytoskeleton is implicated in numerous processes such as cellular division, migration, endocytosislexocytosis, and more recently synaptic plasticity. Important players in controlling cytoskeletal rearrangements are the Cyclase Associated Proteins (CAPs) which are thought to link cell signalling to the dynamics of the actin cytoskeleton, via sequestration of monomeric actin subunits. CAPs are conserved throughout evolution and possess conserved functional domains. Previous studies have suggested a link between CAP proteins and vesicle trafficking and this study focussed on characterizing binding partners of human CAPs. Using a two hybrid screen of a human adult brain cDNA library, a novel human CAP interacting protein named Neuronal calcium binding protein 1 (Necab1) has been isolated. Necab1 is a 351 amino acid protein containing a predicted calcium binding EF-hand and three coiled-coil domains. It is highly expressed in human brain, and similar to CAP2, displays high levels of expression within the hippocampus and cerebral cortex of rat brain. In vitro binding and in vivo immunoprecipitations demonstrate that CAP2 interacts with Necab1. (Abstract shortened by UMI.)Dept. of Biological Sciences. Paper copy at Leddy Library: Theses & Major Papers - Basement, West Bldg. / Call Number: Thesis2002 .M68. Source: Masters Abstracts International, Volume: 43-01, page: 0215. Adviser: A. V. Hubberstey. Thesis (M.Sc.)--University of Windsor (Canada), 2003.
Recommended Citation
Mottillo, Emilio P., "Characterization of a novel human CAP2 interacting protein: Neuronal calcium binding protein 1 (Necab1)." (2003). Electronic Theses and Dissertations. 1396.
https://scholar.uwindsor.ca/etd/1396