Premium
Analysis of the structure of cortactin by native gel electrophoresis
Author(s) -
Petrovich Jessica,
Kruchten Anne E
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.883.5
Subject(s) - cortactin , phosphorylation , mutant , motility , chemistry , gel electrophoresis , microbiology and biotechnology , actin , biophysics , biochemistry , biology , cytoskeleton , gene , cell
Cortactin is an actin‐binding protein that acts as a Src‐kinase substrate and has been shown to be involved in cellular migration and metastases. Previous studies have shown that cortactin is an elongated protein with limited tertiary structure. It is understood that phosphorylation of cortactin affects its role in cellular motility and metastases but the mechanism for this remains unknown. We hypothesize that phosphorylation induces a conformational change in the folding pattern of cortactin. Non‐denaturing acrylamide electrophoresis gels (native gels) were run of mutant phosphorylation‐inhibiting and mocking mutants of cortactin and compared to wild type. We found differences in the migration of bands between the wild type and mutant forms, suggesting conformational differences between them. This work was supported by a Faculty Start Up Grant to A.E. Kruchten by The Murdock Charitable Trust and by a Linfield College Faculty Student Collaborative Research Award to A.E. Kruchten and J. Petrovich.