Signal-Transducing Adaptor Protein-2 Regulates Stromal Cell-Derived Factor-1α-Induced Chemotaxis in T Cells
Author(s) -
Yuichi Sekine,
Osamu Ikeda,
Satoshi Tsuji,
Chikako Yamamoto,
Ryuta Muromoto,
Asuka Nanbo,
Kenji Oritani,
Akihiko Yoshimura,
Tadashi Matsuda
Publication year - 2009
Publication title -
the journal of immunology
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 2.737
H-Index - 372
eISSN - 1550-6606
pISSN - 0022-1767
DOI - 10.4049/jimmunol.0902096
Subject(s) - signal transducing adaptor protein , jurkat cells , rac1 , guanine nucleotide exchange factor , microbiology and biotechnology , cdc42 , pleckstrin homology domain , chemotaxis , signal transduction , cell migration , stromal cell , biology , chemistry , t cell , cell , receptor , cancer research , biochemistry , immunology , immune system
Signal-transducing adaptor protein-2 (STAP-2) is a recently identified adaptor protein that contains pleckstrin and Src homology 2-like domains, as well as a YXXQ motif in its C-terminal region. Our previous studies revealed that STAP-2 regulates integrin-mediated T cell adhesion. In the present study, we find that STAP-2 expression affects Jurkat T cell migration after stromal cell-derived factor-1alpha (SDF-1alpha)-treatment. Furthermore, STAP-2-deficient T cells exhibit reduced cell migration after SDF-1alpha-treatment. Importantly, overexpression of STAP-2 in Jurkat T cells induces activation of small guanine triphosphatases, such as Rac1 and Cdc42. Regarding the mechanism for this effect, we found that STAP-2 associates with Vav1, the guanine-nucleotide exchanging factor for Rac1, and enhances downstream Vav1/Rac1 signaling. These results reveal a novel STAP-2-mediated mechanism for the regulation of SDF-1alpha-induced chemotaxis of T cells via activation of Vav1/Rac1 signaling.
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