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CD98 induces LFA‐1‐mediated cell adhesion in lymphoid cells via activation of Rap1
Author(s) -
Suga Koji,
Katagiri Koko,
Kinashi Tatsuo,
Harazaki Masashi,
Iizuka Tadahiko,
Hattori Masakazu,
Minato Nagahiro
Publication year - 2001
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/s0014-5793(00)02222-5
Subject(s) - rap1 , microbiology and biotechnology , cell adhesion , chemistry , adhesion , gtpase , small gtpase , signal transduction , biology , cell , biochemistry , organic chemistry
CD98 is a multifunctional heterodimeric membrane protein involved in the regulation of cell adhesion as well as amino acid transport. We show that CD98 cross‐linking persistently activates Rap1 GTPase in a LFA‐1‐dependent manner and induces LFA‐1/ICAM‐1‐mediated cell adhesion in lymphocytes. Specific phosphatidylinositol‐3‐kinase (PI3K) inhibitors suppressed both LFA‐1 activation and Rap1GTP generation, and abrogation of Rap1GTP by retroviral over‐expression of a specific Rap1 GTPase activating protein, SPA‐1, totally inhibited the LFA‐1/ICAM‐1‐mediated cell adhesion. These results suggest that CD98 cross‐linking activates LFA‐1 via the PI3K signaling pathway and induces accumulation of Rap1GTP in a LFA‐1‐dependent manner, which in turn mediates the cytoskeleton‐dependent cell adhesion process.