Premium
The actin binding protein cortactin behaves as an intrinsically unstructured protein
Author(s) -
Kruchten Anne E
Publication year - 2008
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.22.1_supplement.1010.4
Subject(s) - cortactin , circular dichroism , stokes radius , size exclusion chromatography , chemistry , phosphorylation , protein secondary structure , globular protein , biophysics , biology , biochemistry , cytoskeleton , cell , enzyme
Cortactin is an actin binding protein known to be involved in several cancer metastases. The experimentally derived weight of 80/85 kDa is in direct contradiction to its theoretically derived molecular weight of approximately 60 kDa. Previously it was reported that cortactin has a larger Stokes radius than predicted for a protein of its size. These data taken together suggest that cortactin does not behave as a typical globular protein but rather as an intrinsically unstructured protein (IUP). Here it is reported that based on the results of computations by computer based algorithms and size exclusion chromatography, cortactin is predicted to have a number of unfolded regions. Phosphorylation of cortactin affects its role in cellular metastases, and it was hypothesized that this may be via modulations of the protein structure, similar to other IUPs. Stokes radii of phosphorylation mutants were analyzed by size exclusion chromatography and compared to wild type. In the future, cortactin structure will be analyzed by biophysical methods such as circular dichroism spectroscopy. This work is supported by a Faculty Start‐Up award from the M.J. Murdock Charitable Trust to A. E. Kruchten.