期刊
MOLECULAR BIOLOGY OF THE CELL
卷 27, 期 9, 页码 1420-1430出版社
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E15-12-0833
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资金
- American Heart Association Postdoctoral Fellowship [15POST24470070]
- National Institutes of Health [GM029860, GM103723, HL114388]
Junctional adhesion molecule A (JAM-A) is a broadly expressed adhesion molecule that regulates cell-cell contacts and facilitates leukocyte transendothelial migration. The latter occurs through interactions with the integrin LFA-1. Although we understand much about JAM-A, little is known regarding the protein's role in mechanotransduction or as a modulator of RhoA signaling. We found that tension imposed on JAM-A activates RhoA, which leads to increased cell stiffness. Activation of RhoA in this system depends on PI3K-mediated activation of GEF-H1 and p115 RhoGEF. These two GEFs are further regulated by FAK/ERK and Src family kinases, respectively. Finally, we show that phosphorylation of JAM-A at Ser-284 is required for RhoA activation in response to tension. These data demonstrate a direct role of JAM-A in mechanosignaling and control of RhoA and implicate Src family kinases in the regulation of p115 RhoGEF.
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