Src kinase-associated phosphoprotein 1 (SKAP1)

Src kinase-associated phosphoprotein 1 (SKAP1) is an intracellular adaptor protein principally expressed in T cells and NK cells. It contains a unique N-terminal dimerization (DM) domain, pleckstrin homology (PH) domain, and C-terminal SH3 domain. SKAP1 plays a critical role in T-cell receptor (TCR) signaling, principally by regulating integrin-mediated adhesion (especially LFA-1 activation) and stabilizing the immunological synapse. Mechanistically, SKAP1 links antigen stimulation to integrin activation via interactions with proteins such as ADAP and RapL, facilitating recruitment to the plasma membrane. It also interacts with Polo-like kinase 1 (PLK1), regulating mitosis and cell cycling during T-cell clonal expansion. Dysfunction or dysregulation of SKAP1 is associated with impaired immune responses and has been linked to various cancers, both as a contributor to oncogenic signaling and as a potential biomarker. While not currently a direct drug target, SKAP1 is implicated as a potential node for therapeutic intervention in cancer and immune-related disorders[1][2][3][4].

Other names

SKAP55SKAP-55SCAP1pp55Src family-associated phosphoprotein 1Src kinase-associated phosphoprotein of 55 kDaHEL-S-81pepididymis secretory sperm binding protein Li 81p

null (therapeutic mechanisms remain investigational; SKAP1 is not a direct drug target, but its pathways and interactions may be modulated indirectly)