GIPC1: Difference between revisions

'''GIPC PDZ domain containing family, member 1''' ('''GIPC1''') is a [[protein]] that in humans is encoded by the ''GIPC1'' [[gene]].<ref name="pmid9770488">{{cite journal | vauthors = De Vries L, Lou X, Zhao G, Zheng B, Farquhar MG | title = GIPC, a PDZ domain containing protein, interacts specifically with the C terminus of RGS-GAIP | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 95 | issue = 21 | pages = 12340–5 | date = November 1998 | pmid = 9770488 | pmc = 22833 | doi = 10.1073/pnas.95.21.12340 | bibcode = 1998PNAS...9512340D | doi-access = free }}</ref><ref name="pmid9482110">{{cite journal | vauthors = Rousset R, Fabre S, Desbois C, Bantignies F, Jalinot P | title = The C-terminus of the HTLV-1 Tax oncoprotein mediates interaction with the PDZ domain of cellular proteins | journal = Oncogene | volume = 16 | issue = 5 | pages = 643–54 | date = March 1998 | pmid = 9482110 | pmc = | doi = 10.1038/sj.onc.1201567 | doi-access = free }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: GIPC1 GIPC PDZ domain containing family, member 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10755| access-date = }}</ref> 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.<ref name="pmid9770488"/> 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&nbsp;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.<ref name = "pmid12011974">{{cite journal | vauthors = Katoh M | title = GIPC gene family (Review) | journal = Int. J. Mol. Med. | volume = 9 | issue = 6 | pages = 585–9 | year = 2002 | pmid = 12011974 | doi = 10.3892/ijmm.9.6.585 }}</ref> 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.

* [[Beta-1 adrenergic receptor|ADRB1]],<ref name = pmid12724327>{{cite journal | vauthors = Hu LA, Chen W, Martin NP, Whalen EJ, Premont RT, Lefkowitz RJ | title = GIPC interacts with the beta1-adrenergic receptor and regulates beta1-adrenergic receptor-mediated ERK activation | journal = J. Biol. Chem. | volume = 278 | issue = 28 | pages = 26295–301 | date = July 2003 | pmid = 12724327 | doi = 10.1074/jbc.M212352200 | doi-access = free }}</ref>

* [[ITGA5]],<ref name = pmid11479315>{{cite journal | vauthors = Tani TT, Mercurio AM | title = 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 | journal = J. Biol. Chem. | volume = 276 | issue = 39 | pages = 36535–42 | date = September 2001 | pmid = 11479315 | doi = 10.1074/jbc.M105785200 | doi-access = free }}</ref>

* [[LRP2]],<ref name = pmid10827173>{{cite journal | vauthors = Gotthardt M, Trommsdorff M, Nevitt MF, Shelton J, Richardson JA, Stockinger W, Nimpf J, Herz J | title = 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 | journal = J. Biol. Chem. | volume = 275 | issue = 33 | pages = 25616–24 | date = August 2000 | pmid = 10827173 | doi = 10.1074/jbc.M000955200 | doi-access = free }}</ref><ref name = pmid12508107>{{cite journal | vauthors = Petersen HH, Hilpert J, Militz D, Zandler V, Jacobsen C, Roebroek AJ, Willnow TE | title = Functional interaction of megalin with the megalinbinding protein (MegBP), a novel tetratrico peptide repeat-containing adaptor molecule | journal = J. Cell. Sci. | volume = 116 | issue = Pt 3 | pages = 453–61 | date = February 2003 | pmid = 12508107 | doi = 10.1242/jcs.00243| doi-access = free }}</ref><ref name = pmid11912251>{{cite journal | vauthors = Lou X, McQuistan T, Orlando RA, Farquhar MG | title = GAIP, GIPC and Galphai3 are concentrated in endocytic compartments of proximal tubule cells: putative role in regulating megalin's function | journal = J. Am. Soc. Nephrol. | volume = 13 | issue = 4 | pages = 918–27 | date = April 2002 | doi = 10.1681/ASN.V134918 | pmid = 11912251 | doi-access = free }}</ref>

* [[Luteinizing hormone/choriogonadotropin receptor|LHCGR]],<ref name = pmid14507927>{{cite journal | vauthors = Hirakawa T, Galet C, Kishi M, Ascoli M | title = GIPC binds to the human lutropin receptor (hLHR) through an unusual PDZ domain binding motif, and it regulates the sorting of the internalized human choriogonadotropin and the density of cell surface hLHR | journal = J. Biol. Chem. | volume = 278 | issue = 49 | pages = 49348–57 | date = December 2003 | pmid = 14507927 | doi = 10.1074/jbc.M306557200 | doi-access = free }}</ref>

* [[MYO6]],<ref name = pmid17353931>{{cite journal | vauthors = Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D | title = Large-scale mapping of human protein-protein interactions by mass spectrometry | journal = Mol. Syst. Biol. | volume = 3 | issue = | pages = 89 | year = 2007 | pmid = 17353931 | pmc = 1847948 | doi = 10.1038/msb4100134 }}</ref><ref name = pmid12857860>{{cite journal | vauthors = Aschenbrenner L, Lee T, Hasson T | title = Myo6 facilitates the translocation of endocytic vesicles from cell peripheries | journal = Mol. Biol. Cell | volume = 14 | issue = 7 | pages = 2728–43 | date = July 2003 | pmid = 12857860 | pmc = 165672 | doi = 10.1091/mbc.E02-11-0767 }}</ref>

* [[TYRP1]].<ref name = pmid11441007>{{cite journal | vauthors = Liu TF, Kandala G, Setaluri V | title = PDZ domain protein GIPC interacts with the cytoplasmic tail of melanosomal membrane protein gp75 (tyrosinase-related protein-1) | journal = J. Biol. Chem. | volume = 276 | issue = 38 | pages = 35768–77 | date = September 2001 | pmid = 11441007 | doi = 10.1074/jbc.M103585200 | doi-access = free }}</ref>

* {{cite journal | vauthors = Hasson T | title = Myosin VI: two distinct roles in endocytosis | journal = J. Cell. Sci. | volume = 116 | issue = Pt 17 | pages = 3453–61 | year = 2003 | pmid = 12893809 | doi = 10.1242/jcs.00669 | doi-access = free }}

* {{cite journal | vauthors = Gress TM, Müller-Pillasch F, Geng M, Zimmerhackl F, Zehetner G, Friess H, Büchler M, Adler G, Lehrach H | title = A pancreatic cancer-specific expression profile | journal = Oncogene | volume = 13 | issue = 8 | pages = 1819–30 | year = 1996 | pmid = 8895530 | doi = }}

* {{cite journal | vauthors = De Vries L, Elenko E, Hubler L, Jones TL, Farquhar MG | title = GAIP is membrane-anchored by palmitoylation and interacts with the activated (GTP-bound) form of G alpha i subunits | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 93 | issue = 26 | pages = 15203–8 | year = 1996 | pmid = 8986788 | pmc = 26381 | doi = 10.1073/pnas.93.26.15203 | bibcode = 1996PNAS...9315203D | doi-access = free }}

* {{cite journal | vauthors = Wang LH, Kalb RG, Strittmatter SM | title = A PDZ protein regulates the distribution of the transmembrane semaphorin, M-SemF | journal = J. Biol. Chem. | volume = 274 | issue = 20 | pages = 14137–46 | year = 1999 | pmid = 10318831 | doi = 10.1074/jbc.274.20.14137 | doi-access = free }}

* {{cite journal | vauthors = Cai H, Reed RR | title = 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 | journal = J. Neurosci. | volume = 19 | issue = 15 | pages = 6519–27 | year = 1999 | pmid = 10414980 | doi = 10.1523/JNEUROSCI.19-15-06519.1999| pmc = 6782790 | doi-access = free }}

* {{cite journal | vauthors = Gotthardt M, Trommsdorff M, Nevitt MF, Shelton J, Richardson JA, Stockinger W, Nimpf J, Herz J | title = 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 | journal = J. Biol. Chem. | volume = 275 | issue = 33 | pages = 25616–24 | year = 2000 | pmid = 10827173 | doi = 10.1074/jbc.M000955200 | doi-access = free }}

* {{cite journal | vauthors = Gao Y, Li M, Chen W, Simons M | title = Synectin, syndecan-4 cytoplasmic domain binding PDZ protein, inhibits cell migration | journal = J. Cell. Physiol. | volume = 184 | issue = 3 | pages = 373–9 | year = 2000 | pmid = 10911369 | doi = 10.1002/1097-4652(200009)184:3<373::AID-JCP12>3.0.CO;2-I | s2cid = 20829740 }}

* {{cite journal | vauthors = Von Kap-Herr C, Kandala G, Mann SS, Hart TC, Pettenati MJ, Setaluri V | title = Assignment of PDZ domain-containing protein GIPC gene (C19orf3) to human chromosome band 19p13.1 by in situ hybridization and radiation hybrid mapping | journal = Cytogenet. Cell Genet. | volume = 89 | issue = 3-43–4 | pages = 234–5 | year = 2000 | pmid = 10965131 | doi = 10.1159/000015621 | s2cid = 85292825 }}

* {{cite journal | vauthors = Liu TF, Kandala G, Setaluri V | title = PDZ domain protein GIPC interacts with the cytoplasmic tail of melanosomal membrane protein gp75 (tyrosinase-related protein-1) | journal = J. Biol. Chem. | volume = 276 | issue = 38 | pages = 35768–77 | year = 2001 | pmid = 11441007 | doi = 10.1074/jbc.M103585200 | doi-access = free }}

* {{cite journal | vauthors = Ligensa T, Krauss S, Demuth D, Schumacher R, Camonis J, Jaques G, Weidner KM | title = A PDZ domain protein interacts with the C-terminal tail of the insulin-like growth factor-1 receptor but not with the insulin receptor | journal = J. Biol. Chem. | volume = 276 | issue = 36 | pages = 33419–27 | year = 2001 | pmid = 11445579 | doi = 10.1074/jbc.M104509200 | doi-access = free }}

* {{cite journal | vauthors = Tani TT, Mercurio AM | title = 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 | journal = J. Biol. Chem. | volume = 276 | issue = 39 | pages = 36535–42 | year = 2001 | pmid = 11479315 | doi = 10.1074/jbc.M105785200 | doi-access = free }}

* {{cite journal | vauthors = Blobe GC, Liu X, Fang SJ, How T, Lodish HF | title = 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 | journal = J. Biol. Chem. | volume = 276 | issue = 43 | pages = 39608–17 | year = 2001 | pmid = 11546783 | doi = 10.1074/jbc.M106831200 | doi-access = free }}

* {{cite journal | vauthors = Lou X, McQuistan T, Orlando RA, Farquhar MG | title = GAIP, GIPC and Galphai3 are concentrated in endocytic compartments of proximal tubule cells: putative role in regulating megalin's function | journal = J. Am. Soc. Nephrol. | volume = 13 | issue = 4 | pages = 918–27 | year = 2002 | doi = 10.1681/ASN.V134918 | pmid = 11912251 | doi-access = free }}