Premium
Post‐translational modification of the RhoGTPase activating protein 21, ARHGAP21, by SUMO2/3
Author(s) -
Bigarella Carolina L.,
Vieira Ferro Karla P.,
Barcellos Karin S.A.,
Martins-de-Souza Daniel,
Traina Fabiola,
Novello José C.,
Olalla Saad Sara T.,
Archangelo Leticia Fröhlich
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.08.012
Subject(s) - sumo protein , cdc42 , microbiology and biotechnology , cytoplasm , biology , lysine , immunofluorescence , chemistry , biochemistry , actin , ubiquitin , genetics , gene , antibody , amino acid
ARHGAP21 is a 217 kDa RhoGAP protein shown to modulate cell migration through the control of Cdc42 and FAK activities. In the present work a 250 kDa‐ARHGAP21 was identified by mass spectrometry. This modified form is differentially expressed among cell lines and human primary cells. Co‐immunoprecipitations and in vitro SUMOylation confirmed ARHGAP21 specific modification by SUMO2/3 and mapped the SUMOylation site to ARHGAP21 lysine K1443. Immunofluorescence staining revealed that ARHGAP21 co‐localizes with SUMO2/3 in the cytoplasm and membrane compartments. Interestingly, our results suggest that ARHGAP21 SUMOylation may be related to cell proliferation. Therefore, SUMOylation of ARHGAP21 may represent a way of guiding its function.