SLP adaptor and CSK interacting membrane protein (SCIMP)

SLP adaptor and CSK interacting membrane protein (SCIMP) is a transmembrane adaptor protein specifically expressed in antigen-presenting cells such as B cells, dendritic cells, and macrophages, and is a constituent of tetraspanin-enriched membrane microdomains. SCIMP participates in immune synapse formation and is involved in major histocompatibility complex class II (MHC-II) signaling. Upon MHC-II stimulation, SCIMP becomes tyrosine phosphorylated, enabling it to recruit signaling adaptors like SLP65/SLP76 and Grb2, as well as the inhibitory kinase Csk. SCIMP also serves as a scaffold for the recruitment of Erk1/2 kinases to TLR4 signaling domains in macrophages, linking membrane events to downstream pro-inflammatory responses, such as cytokine production[1][2][3][4][5]. SCIMP is not classified as a classical receptor, enzyme, or transporter, but as a key regulatory adaptor molecule for immune cell signaling. There are no documented clinical drugs specifically targeting SCIMP as of now. Its expression is correlated with immune cell activation, particularly in cells expressing MHC class II molecules.

Other names

C17orf87SLP65/SLP76, Csk-interacting membrane proteintransmembrane protein C17orf87UNQ5783/PRO16090DTFT5783FLJ32580MGC163426MGC163428