PID1 (PTB-containing, cubilin and LRP1-interacting protein; also known as NYGGF4) is a phosphotyrosine-binding (PTB) domain-containing protein. It is an inhibitor of insulin-mediated signaling in adipocytes and muscle cells. It binds through its PTB domain to the second NPXY motif in the cytoplasmic tail of the low density lipoprotein receptor-related protein 1 (LRP1)[]. Besides being involved in obesity-associated insulin resistance [], PID1 has been shown to inhibit growth of medulloblastoma, glioblastoma and atypical teratoid rhabdoid tumour cell lines [].
PID1 (PTB-containing, cubilin and LRP1-interacting protein; also known as NYGGF4) is a phosphotyrosine-binding (PTB) domain-containing protein. It is an inhibitor of insulin-mediated signaling in adipocytes and muscle cells. It binds through its PTB domain to the second NPXY motif in the cytoplasmic tail of the low density lipoprotein receptor-related protein 1 (LRP1)[]. Besides being involved in obesity-associated insulin resistance [], PID1 has been shown to inhibit growth of medulloblastoma, glioblastoma and atypical teratoid rhabdoid tumour cell lines [].This entry represents the PTB domain of PID1.Proteins encoding phosphotyrosine binding (PTB) domains function as adaptors or scaffolds to organise the signaling complexes involved in wide-ranging physiological processes including neural development, immunity, tissue homeostasis and cell growth. Due to structural differences, PTB domains are divided into three groups represented by phosphotyrosine-dependent IRS-like, phosphotyrosine-dependent Shc-like, and phosphotyrosine-independent Dab-like PTBs. The last two PTBs have been named as phosphotyrosine interaction domain (PID or PI domain). PID domain has an average length of about 160 amino acids [].
