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Caspase‐3 digestion of cortactin: Analysis of Cortactin Structure
Author(s) -
Foster Jeneva,
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.883.4
Subject(s) - cortactin , phosphorylation , mutant , folding (dsp implementation) , wild type , chemistry , protein folding , in vitro , microbiology and biotechnology , biology , biochemistry , cell , cytoskeleton , gene , electrical engineering , engineering
Cortactin is a Src substrate protein that interacts with actin, and is involved in several types of cancer metastases. Phosphorylation of cortactin by Src and Erk affects its role in cancer metastases, possibly via induced changes in the folding of the protein. To test if phosphorylation alters the structure of the protein, wild type and two mutants (one to mimic, and one to block phosphorylation) were digested in‐vitro with the protease caspase‐3, which has two potential target sites on cortactin. Cortactin was digested at varying times and with varying concentrations of caspase‐3 in reaction; results showed that the wild type and mutant proteins were digested at varying rates. We hypothesize variation in digestion is a result of different folding patterns between wild type and mutants due to either an exposed target site or a target site buried within the structure of the protein. 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. Foster.