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Src-like adapter protein 2 (SLAP2) is a non-enzymatic adaptor protein encoded by the SLA2 gene located on chromosome 20 in humans[1][3]. It is primarily expressed in hematopoietic tissues and contains an N-terminal myristoylation motif that allows membrane association, as well as Src Homology 2 (SH2) and Src Homology 3 (SH3) domains for protein-protein interactions[4][5]. SLAP2 plays an important role as a negative regulator of immune receptor signaling by inhibiting antigen receptor-induced signaling cascades in T and B lymphocytes, partially through recruitment of the ubiquitin ligase Cbl, which promotes ubiquitination and degradation of activated receptors such as KIT, CSF1R, and FLT3[2][4]. Deficiency or dysregulation of SLAP2 has been implicated in immune dysfunction and malignancy due to impaired modulation of signaling pathways. SLAP2 itself is not a direct therapeutic target, but its regulatory roles may be relevant for diseases involving disordered immune signaling and oncogenic activation of receptor tyrosine kinases[2][5].
Not a therapeutic target, but functions as an adaptor protein that recruits the E3 ubiquitin ligase Cbl, promoting degradation of activated signaling receptors
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