Src-like adaptor protein (SLAP)

Src-like adaptor protein (SLAP) is a cytoplasmic signaling adaptor that contains SH2 and SH3 domains similar to the Src family kinases but lacks tyrosine kinase activity due to its unique C-terminal region. SLAP plays a crucial role as a negative regulator of multiple cell surface receptor signaling pathways, including T cell and B cell receptors, cytokine receptors, and receptor tyrosine kinases such as EPHA2, FLT3, c-KIT, PDGFR, EPOR, and CSF1R. By recruiting ubiquitin ligases (notably CBL), SLAP promotes ubiquitination and degradation of associated receptors or kinases, thereby attenuating signaling. SLAP’s primary biological functions include regulation of immune cell development, prevention of excessive cell proliferation and activation, and maintenance of immune tolerance. SLAP is expressed in many tissues, with a prominent role in lymphocytes but also influences diverse processes including osteoporosis and cancer. SLAP loss or downregulation is observed in some cancers, where it can function as a tumor suppressor. There are two homologous proteins in humans—SLAP (SLA) and SLAP-2 (SLA2). The provided name "Src like adaptor" is ambiguous, but most often, literature refers to SLAP/SLA as “Src-like adaptor protein.”

Other names

Src-like adaptor proteinSLAPSrc-like adapterSLAP-1SLA

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