Semester
Summer
Date of Graduation
2002
Document Type
Thesis
Degree Type
MS
College
School of Medicine
Department
Microbiology, Immunology, and Cell Biology
Committee Chair
Daniel Flynn.
Abstract
As there are over twenty potential PKC phosphorylation sites in AFAP-110 structure, deletional mutagenesis was employed to determine which regions of AFAP-110 are most likely to contain crucial sites for PKC phosphorylation. Our data indicate that functional PKC phosphorylation sites must be localized to the amino acid stretch 266--294 within STK region of AFAP-110. There are four PKC candidate phosphorylation sites in this region; they are being substituted by alanine residues in order to determine their significance in serine/threonine phosphorylation regulation of AFAP-110 function.;Analysis of AFAP-110 amino acid sequence has also revealed that AFAP-110 contains twelve potential 14-3-3 binding sequences. 14-3-3 proteins are a family of small acidic adaptor proteins of dimeric nature that act as molecular scaffolds and/or allosteric regulators in a number of cellular pathways. We have been interested to determine whether 14-3-3 is a binding partner for AFAP-110 in vivo. We determined that AFAP-110 associates with 14-3-3 in vivo, although it still remains unknown whether this association is direct or facilitated by any of a multitude of 14-3-3 binding partners. (Abstract shortened by UMI.).
Recommended Citation
Cherezova, Lidia Nikolayevna, "Determining the effects of phosphorylation on AFAP-110 function" (2002). Graduate Theses, Dissertations, and Problem Reports. 1517.
https://researchrepository.wvu.edu/etd/1517