Biology:GIPC1

Short description: Protein-coding gene in the species Homo sapiens

Generic protein structure example

GIPC PDZ domain containing family, member 1 (GIPC1) is a protein that in humans is encoded by the GIPC1 gene. GIPC was originally identified as it binds specifically to the C terminus of RGS-GAIP, a protein involved in the regulation of G protein signaling. GIPC is an acronym for "GAIP Interacting Protein C-terminus". RGS proteins are "Regulators of G protein Signaling" and RGS-GAIP is a "GTPase Activator protein for Gαi/Gαq", which are two major subtypes of Gα proteins. The human GIPC1 molecule is 333 amino acids or about 36 kDa in molecular size and consists of a central PDZ domain, a compact protein module which mediates specific protein-protein interactions. The RGS-GAIP protein interacts with this domain and many other proteins interact here or at other parts of the GIPC1 molecule. As a result, GIPC1 was independently discovered by several other groups and has a variety of alternate names, including synectin, C19orf3, RGS19IP1 and others. The GIPC1 gene family in mammals consisting of three members, so the first discovered, originally named GIPC, is now generally called GIPC1, with the other two being named GIPC2 and GIPC3. The three human proteins are about 60% identical in protein sequence. GIPC1 has been shown to interact with a variety of other receptor and cytoskeletal proteins including the GLUT1 receptor, ACTN1, KIF1B, MYO6, PLEKHG5, SDC4/syndecan-4, SEMA4C/semaphorin-4 and HTLV-I Tax. The general function of GIPC family proteins therefore appears to be mediating specific interactions between proteins involved in G protein signaling and membrane translocation.

Interactions

GIPC1 has been shown to interact with:

• Actinin, alpha 1,
• ADRB1,
• GLUT1,
• ITGA5,
• ITGA6,
• KIF1B,
• LRP1,
• LRP2,
• LHCGR,
• MYO6,
• RGS19,
• TPBG, and
• TYRP1.

See also

GIPC PDZ domain containing family, member 2, GIPC2

GIPC PDZ domain containing family, member 3, GIPC3

Further reading

• "GIPC gene family (Review)". Int. J. Mol. Med. 9 (6): 585–9. 2002. doi:10.3892/ijmm.9.6.585. PMID 12011974. 
• "Myosin VI: two distinct roles in endocytosis". J. Cell Sci. 116 (Pt 17): 3453–61. 2003. doi:10.1242/jcs.00669. PMID 12893809. 
• "A pancreatic cancer-specific expression profile". Oncogene 13 (8): 1819–30. 1996. PMID 8895530. 
• "GAIP is membrane-anchored by palmitoylation and interacts with the activated (GTP-bound) form of G alpha i subunits". Proc. Natl. Acad. Sci. U.S.A. 93 (26): 15203–8. 1996. doi:10.1073/pnas.93.26.15203. PMID 8986788. Bibcode: 1996PNAS...9315203D. 
• "Protein interactions with the glucose transporter binding protein GLUT1CBP that provide a link between GLUT1 and the cytoskeleton". Mol. Biol. Cell 10 (4): 819–32. 1999. doi:10.1091/mbc.10.4.819. PMID 10198040. 
• "A PDZ protein regulates the distribution of the transmembrane semaphorin, M-SemF". J. Biol. Chem. 274 (20): 14137–46. 1999. doi:10.1074/jbc.274.20.14137. PMID 10318831. 
• "Cloning and characterization of neuropilin-1-interacting protein: a PSD-95/Dlg/ZO-1 domain-containing protein that interacts with the cytoplasmic domain of neuropilin-1". J. Neurosci. 19 (15): 6519–27. 1999. doi:10.1523/JNEUROSCI.19-15-06519.1999. PMID 10414980. 
• "Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest diverse biological functions in cellular communication and signal transduction". J. Biol. Chem. 275 (33): 25616–24. 2000. doi:10.1074/jbc.M000955200. PMID 10827173. 
• "Synectin, syndecan-4 cytoplasmic domain binding PDZ protein, inhibits cell migration". J. Cell. Physiol. 184 (3): 373–9. 2000. doi:10.1002/1097-4652(200009)184:3<373::AID-JCP12>3.0.CO;2-I. PMID 10911369. 
• "Assignment of PDZ domain-containing protein GIPC gene (C19orf3) to human chromosome band 19p13.1 by in situ hybridization and radiation hybrid mapping". Cytogenet. Cell Genet. 89 (3–4): 234–5. 2000. doi:10.1159/000015621. PMID 10965131. 
• "GIPC and GAIP form a complex with TrkA: a putative link between G protein and receptor tyrosine kinase pathways". Mol. Biol. Cell 12 (3): 615–27. 2001. doi:10.1091/mbc.12.3.615. PMID 11251075. 
• "PDZ domain protein GIPC interacts with the cytoplasmic tail of melanosomal membrane protein gp75 (tyrosinase-related protein-1)". J. Biol. Chem. 276 (38): 35768–77. 2001. doi:10.1074/jbc.M103585200. PMID 11441007. 
• "A PDZ domain protein interacts with the C-terminal tail of the insulin-like growth factor-1 receptor but not with the insulin receptor". J. Biol. Chem. 276 (36): 33419–27. 2001. doi:10.1074/jbc.M104509200. PMID 11445579. 
• "PDZ interaction sites in integrin alpha subunits. T14853, TIP/GIPC binds to a type I recognition sequence in alpha 6A/alpha 5 and a novel sequence in alpha 6B". J. Biol. Chem. 276 (39): 36535–42. 2001. doi:10.1074/jbc.M105785200. PMID 11479315. 
• "A novel mechanism for regulating transforming growth factor beta (TGF-beta) signaling. Functional modulation of type III TGF-beta receptor expression through interaction with the PDZ domain protein, GIPC". J. Biol. Chem. 276 (43): 39608–17. 2001. doi:10.1074/jbc.M106831200. PMID 11546783. 
• "5T4 interacts with TIP-2/GIPC, a PDZ protein, with implications for metastasis". Biochem. Biophys. Res. Commun. 290 (3): 1030–6. 2002. doi:10.1006/bbrc.2001.6288. PMID 11798178. 
• "The PDZ domain of TIP-2/GIPC interacts with the C-terminus of the integrin alpha5 and alpha6 subunits". Matrix Biol. 21 (2): 207–14. 2002. doi:10.1016/S0945-053X(01)00198-6. PMID 11852236. 
• "GAIP, GIPC and Galphai3 are concentrated in endocytic compartments of proximal tubule cells: putative role in regulating megalin's function". J. Am. Soc. Nephrol. 13 (4): 918–27. 2002. doi:10.1681/ASN.V134918. PMID 11912251.