Journal
IMMUNOLOGICAL REVIEWS
Volume 218, Issue -, Pages 65-81Publisher
WILEY
DOI: 10.1111/j.1600-065X.2007.00527.x
Keywords
integrin; signal transduction; adapter protein; T-cell receptor; T-cell activation; adhesion
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Funding
- NIAID NIH HHS [R01 AI038474, R01 AI031126] Funding Source: Medline
- NIDCR NIH HHS [T32 DE007288] Funding Source: Medline
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Integrin adhesion receptors are critical for antigen recognition by T cells and for regulated recirculation and trafficking into and through various tissues in the body. T-cell receptor (TCR) signaling induces rapid increases in integrin function that facilitate T-cell activation by promoting stable contact with antigen-presenting cells and extracellular proteins in the environment. In this review, we outline the molecular mechanisms by which the TCR signals to integrins and present a model that highlights four key events: (i) initiation of proximal TCR signals nucleated by the linker for activated T cells (LAT) adapter protein and involving Itk, phospholipase C-gamma 1, Vav1, and Src homology 2 domain-containing leukocyte-specific phosphoprotein of 76 kDa; (ii) transmission of integrin activation signals from the LAT signalosome to integrins by protein kinase (PK) C and the adapter protein, adhesion and degranulation-promoting adapter protein; (iii) assembly of integrin-associated signaling complexes that include PKD, the guanosine triphosphatase Rap1 and its effectors, and talin; and (iv) reorganization of the actin cytoskeleton by WAVE2 and other actin-remodeling proteins. These events coordinate changes in integrin conformation and clustering that result in enhanced integrin functional activity following TCR stimulation.
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