Determining the effects of phosphorylation on AFAP-110 function

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.).

Name thesis:degree_name

MS

Level thesis:degree_level

Thesis

Discipline thesis:degree_discipline

Microbiology, Immunology, and Cell Biology

Year dc:date.available

2002

Author dc:creator

• Cherezova, Lidia Nikolayevna

Contributors dc:contributor

• Daniel Flynn.

• Cellular biology
• Molecular biology

Identifier

https://researchrepository.wvu.edu/etd/1517

OAI identifier oai:identifier

oai:researchrepository.wvu.edu:etd-2520