SH3 domain-binding protein 4 (SH3BP4)

SH3 domain-binding protein 4 (SH3BP4) is an adaptor protein involved in the control of clathrin-mediated endocytosis and the trafficking of the transferrin receptor, containing motifs for interaction with endocytic and signaling proteins, including an SH3 domain, NPF repeats (EH domain-binding sites), and a death domain. SH3BP4 acts as a negative regulator of mTORC1 signaling by binding inactive Rag GTPase complexes, thereby impeding mTORC1 activation in response to amino acids. This regulatory function implicates SH3BP4 as a potential tumor suppressor, as deletions of the SH3BP4 locus are seen in several cancer types. SH3BP4 is highly conserved among vertebrates and is linked to both endosomal trafficking and cell signaling networks[1][2][3][4].

Other names

BOG25EHB10TTPEH-binding protein 10Transferrin receptor-trafficking protein

Inhibition of amino acid-induced activation of mTORC1 by binding inactive Rag GTPase complexes[2][4]