GIPC1: Difference between revisions

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{{Infobox_gene}}
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'''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 }}</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 }}</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.
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Interactions ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =  
| Name = GIPC PDZ domain containing family, member 1
| HGNCid = 1226
| Symbol = GIPC1
| AltSymbols =; C19orf3; GIPC; GLUT1CBP; Hs.6454; IIP-1; MGC15889; MGC3774; NIP; RGS19IP1; SEMCAP; SYNECTIIN; TIP-2
| OMIM = 605072
| ECnumber = 
| Homologene = 21167
| MGIid = 1926252
| GeneAtlas_image1 = PBB_GE_GIPC1_207525_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0005102 |text = receptor binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005625 |text = soluble fraction}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0005938 |text = cell cortex}} {{GNF_GO|id=GO:0008021 |text = synaptic vesicle}} {{GNF_GO|id=GO:0012506 |text = vesicle membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016023 |text = cytoplasmic membrane-bound vesicle}} {{GNF_GO|id=GO:0043197 |text = dendritic spine}} {{GNF_GO|id=GO:0043198 |text = dendritic shaft}}
| Process = {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}} {{GNF_GO|id=GO:0014047 |text = glutamate secretion}} {{GNF_GO|id=GO:0048167 |text = regulation of synaptic plasticity}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 10755
    | Hs_Ensembl = ENSG00000123159
    | Hs_RefseqProtein = NP_005707
    | Hs_RefseqmRNA = NM_005716
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 19
    | Hs_GenLoc_start = 14449572
    | Hs_GenLoc_end = 14467944
    | Hs_Uniprot = O14908
    | Mm_EntrezGene = 67903
    | Mm_Ensembl = ENSMUSG00000019433
    | Mm_RefseqmRNA = NM_018771
    | Mm_RefseqProtein = NP_061241
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 8
    | Mm_GenLoc_start = 86542783
    | Mm_GenLoc_end = 86554894
    | Mm_Uniprot = Q9Z0G0
  }}
}}
'''GIPC PDZ domain containing family, member 1''', also known as '''GIPC1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GIPC1 GIPC PDZ domain containing family, member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10755| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
GIPC1 has been shown to [[Protein-protein interaction|interact]] with:
{{PBB_Summary
{{div col|colwidth=20em}}
| section_title =  
* [[Actinin, alpha 1]],<ref name = pmid10198040/>
| summary_text =  
* [[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 }}</ref>
}}
* [[GLUT1]],<ref name = pmid10198040>{{cite journal | vauthors = Bunn RC, Jensen MA, Reed BC | title = Protein interactions with the glucose transporter binding protein GLUT1CBP that provide a link between GLUT1 and the cytoskeleton | journal = Mol. Biol. Cell | volume = 10 | issue = 4 | pages = 819–32 | date = April 1999 | pmid = 10198040 | pmc = 25204 | doi =  10.1091/mbc.10.4.819}}</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 }}</ref>
* [[ITGA6]],<ref name = pmid11479315/>
* [[KIF1B]],<ref name = pmid10198040/>
* [[LRP1]],<ref name = pmid10827173/>
* [[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 }}</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}}</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 | pmid = 11912251 | doi =  }}</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 }}</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>
* [[RGS19]],<ref name = pmid11251075>{{cite journal | vauthors = Lou X, Yano H, Lee F, Chao MV, Farquhar MG | title = GIPC and GAIP form a complex with TrkA: a putative link between G protein and receptor tyrosine kinase pathways | journal = Mol. Biol. Cell | volume = 12 | issue = 3 | pages = 615–27  | date = March 2001 | pmid = 11251075 | pmc = 30968 | doi =  10.1091/mbc.12.3.615}}</ref>
* [[TPBG]],<ref name = pmid11798178>{{cite journal | vauthors = Awan A, Lucic MR, Shaw DM, Sheppard F, Westwater C, Lyons SA, Stern PL | title = 5T4 interacts with TIP-2/GIPC, a PDZ protein, with implications for metastasis | journal = Biochem. Biophys. Res. Commun. | volume = 290 | issue = 3 | pages = 1030–6  | date = January 2002 | pmid = 11798178 | doi = 10.1006/bbrc.2001.6288 }}</ref>  and
* [[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 }}</ref>
{{Div col end}}


==References==
== See also ==
GIPC PDZ domain containing family, member 2, [[GIPC2]]
 
GIPC PDZ domain containing family, member 3, [[GIPC3]]
 
== References ==
{{reflist|2}}
{{reflist|2}}
==Further reading==
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{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 }}
| citations =
* {{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 }}
*{{cite journal | author=Katoh M |title=GIPC gene family (Review). |journal=Int. J. Mol. Med. |volume=9 |issue= 6 |pages= 585-9 |year= 2002 |pmid= 12011974 |doi= }}
* {{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 | author=Hasson T |title=Myosin VI: two distinct roles in endocytosis. |journal=J. Cell. Sci. |volume=116 |issue= Pt 17 |pages= 3453-61 |year= 2004 |pmid= 12893809 |doi= 10.1242/jcs.00669 }}
* {{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 }}
*{{cite journal | author=Gress TM, Müller-Pillasch F, Geng M, ''et al.'' |title=A pancreatic cancer-specific expression profile. |journal=Oncogene |volume=13 |issue= 8 |pages= 1819-30 |year= 1996 |pmid= 8895530 |doi=  }}
* {{cite journal | vauthors = Bunn RC, Jensen MA, Reed BC | title = Protein interactions with the glucose transporter binding protein GLUT1CBP that provide a link between GLUT1 and the cytoskeleton | journal = Mol. Biol. Cell | volume = 10 | issue = 4 | pages = 819–32 | year = 1999 | pmid = 10198040 | pmc = 25204 | doi = 10.1091/mbc.10.4.819 }}
*{{cite journal | author=De Vries L, Elenko E, Hubler L, ''et al.'' |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= 1997 |pmid= 8986788 |doi= }}
* {{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 }}
*{{cite journal | author=Rousset R, Fabre S, Desbois C, ''et al.'' |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 |year= 1998 |pmid= 9482110 |doi= 10.1038/sj.onc.1201567 }}
* {{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 =  }}
*{{cite journal | author=De Vries L, Lou X, Zhao G, ''et al.'' |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 |year= 1998 |pmid= 9770488 |doi= }}
* {{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 }}
*{{cite journal | author=Bunn RC, Jensen MA, Reed BC |title=Protein interactions with the glucose transporter binding protein GLUT1CBP that provide a link between GLUT1 and the cytoskeleton. |journal=Mol. Biol. Cell |volume=10 |issue= 4 |pages= 819-32 |year= 1999 |pmid= 10198040 |doi=  }}
* {{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 }}
*{{cite journal | author=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= }}
* {{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 = 3-4 | pages = 234–5 | year = 2000 | pmid = 10965131 | doi = 10.1159/000015621 }}
*{{cite journal | author=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= }}
* {{cite journal | vauthors = Lou X, Yano H, Lee F, Chao MV, Farquhar MG | title = GIPC and GAIP form a complex with TrkA: a putative link between G protein and receptor tyrosine kinase pathways | journal = Mol. Biol. Cell | volume = 12 | issue = 3 | pages = 615–27 | year = 2001 | pmid = 11251075 | pmc = 30968 | doi = 10.1091/mbc.12.3.615 }}
*{{cite journal  | author=Gotthardt M, Trommsdorff M, Nevitt MF, ''et al.'' |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 }}
* {{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 }}
*{{cite journal | author=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 }}
* {{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 }}
*{{cite journal | author=Von Kap-Herr C, Kandala G, Mann SS, ''et al.'' |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= 3-4 |pages= 234-5 |year= 2000 |pmid= 10965131 |doi= }}
* {{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 }}
*{{cite journal | author=Lou X, Yano H, Lee F, ''et al.'' |title=GIPC and GAIP form a complex with TrkA: a putative link between G protein and receptor tyrosine kinase pathways. |journal=Mol. Biol. Cell |volume=12 |issue= 3 |pages= 615-27 |year= 2001 |pmid= 11251075 |doi= }}
* {{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 }}
*{{cite journal | author=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 }}
* {{cite journal | vauthors = Awan A, Lucic MR, Shaw DM, Sheppard F, Westwater C, Lyons SA, Stern PL | title = 5T4 interacts with TIP-2/GIPC, a PDZ protein, with implications for metastasis | journal = Biochem. Biophys. Res. Commun. | volume = 290 | issue = 3 | pages = 1030–6 | year = 2002 | pmid = 11798178 | doi = 10.1006/bbrc.2001.6288 }}
*{{cite journal | author=Ligensa T, Krauss S, Demuth D, ''et al.'' |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 }}
* {{cite journal | vauthors = El Mourabit H, Poinat P, Koster J, Sondermann H, Wixler V, Wegener E, Laplantine E, Geerts D, Georges-Labouesse E, Sonnenberg A, Aumailley M | title = The PDZ domain of TIP-2/GIPC interacts with the C-terminus of the integrin alpha5 and alpha6 subunits | journal = Matrix Biol. | volume = 21 | issue = 2 | pages = 207–14 | year = 2002 | pmid = 11852236 | doi = 10.1016/S0945-053X(01)00198-6 }}
*{{cite journal | author=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 }}
* {{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 | pmid = 11912251 | doi =  }}
*{{cite journal | author=Blobe GC, Liu X, Fang SJ, ''et al.'' |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 }}
*{{cite journal | author=Awan A, Lucic MR, Shaw DM, ''et al.'' |title=5T4 interacts with TIP-2/GIPC, a PDZ protein, with implications for metastasis. |journal=Biochem. Biophys. Res. Commun. |volume=290 |issue= 3 |pages= 1030-6 |year= 2002 |pmid= 11798178 |doi= 10.1006/bbrc.2001.6288 }}
*{{cite journal  | author=El Mourabit H, Poinat P, Koster J, ''et al.'' |title=The PDZ domain of TIP-2/GIPC interacts with the C-terminus of the integrin alpha5 and alpha6 subunits. |journal=Matrix Biol. |volume=21 |issue= 2 |pages= 207-14 |year= 2002 |pmid= 11852236 |doi=  }}
*{{cite journal | author=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 |pmid= 11912251 |doi=  }}
}}
{{refend}}
{{refend}}
{{protein-stub}}
{{WikiDoc Sources}}

Revision as of 19:59, 8 November 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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GIPC PDZ domain containing family, member 1 (GIPC1) is a protein that in humans is encoded by the GIPC1 gene.[1][2][3] 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.[1] 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.[4] 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:

See also

GIPC PDZ domain containing family, member 2, GIPC2

GIPC PDZ domain containing family, member 3, GIPC3

References

  1. ↑ 1.0 1.1 De Vries L, Lou X, Zhao G, Zheng B, Farquhar MG (November 1998). "GIPC, a PDZ domain containing protein, interacts specifically with the C terminus of RGS-GAIP". Proc. Natl. Acad. Sci. U.S.A. 95 (21): 12340–5. doi:10.1073/pnas.95.21.12340. PMC 22833. PMID 9770488.
  2. ↑ Rousset R, Fabre S, Desbois C, Bantignies F, Jalinot P (March 1998). "The C-terminus of the HTLV-1 Tax oncoprotein mediates interaction with the PDZ domain of cellular proteins". Oncogene. 16 (5): 643–54. doi:10.1038/sj.onc.1201567. PMID 9482110.
  3. ↑ "Entrez Gene: GIPC1 GIPC PDZ domain containing family, member 1".
  4. ↑ Katoh M (2002). "GIPC gene family (Review)". Int. J. Mol. Med. 9 (6): 585–9. doi:10.3892/ijmm.9.6.585. PMID 12011974.
  5. ↑ 5.0 5.1 5.2 Bunn RC, Jensen MA, Reed BC (April 1999). "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. doi:10.1091/mbc.10.4.819. PMC 25204. PMID 10198040.
  6. ↑ Hu LA, Chen W, Martin NP, Whalen EJ, Premont RT, Lefkowitz RJ (July 2003). "GIPC interacts with the beta1-adrenergic receptor and regulates beta1-adrenergic receptor-mediated ERK activation". J. Biol. Chem. 278 (28): 26295–301. doi:10.1074/jbc.M212352200. PMID 12724327.
  7. ↑ 7.0 7.1 Tani TT, Mercurio AM (September 2001). "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. doi:10.1074/jbc.M105785200. PMID 11479315.
  8. ↑ 8.0 8.1 Gotthardt M, Trommsdorff M, Nevitt MF, Shelton J, Richardson JA, Stockinger W, Nimpf J, Herz J (August 2000). "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. doi:10.1074/jbc.M000955200. PMID 10827173.
  9. ↑ Petersen HH, Hilpert J, Militz D, Zandler V, Jacobsen C, Roebroek AJ, Willnow TE (February 2003). "Functional interaction of megalin with the megalinbinding protein (MegBP), a novel tetratrico peptide repeat-containing adaptor molecule". J. Cell Sci. 116 (Pt 3): 453–61. doi:10.1242/jcs.00243. PMID 12508107.
  10. ↑ Lou X, McQuistan T, Orlando RA, Farquhar MG (April 2002). "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. PMID 11912251.
  11. ↑ Hirakawa T, Galet C, Kishi M, Ascoli M (December 2003). "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". J. Biol. Chem. 278 (49): 49348–57. doi:10.1074/jbc.M306557200. PMID 14507927.
  12. ↑ 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 (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3: 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
  13. ↑ Aschenbrenner L, Lee T, Hasson T (July 2003). "Myo6 facilitates the translocation of endocytic vesicles from cell peripheries". Mol. Biol. Cell. 14 (7): 2728–43. doi:10.1091/mbc.E02-11-0767. PMC 165672. PMID 12857860.
  14. ↑ Lou X, Yano H, Lee F, Chao MV, Farquhar MG (March 2001). "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. doi:10.1091/mbc.12.3.615. PMC 30968. PMID 11251075.
  15. ↑ Awan A, Lucic MR, Shaw DM, Sheppard F, Westwater C, Lyons SA, Stern PL (January 2002). "5T4 interacts with TIP-2/GIPC, a PDZ protein, with implications for metastasis". Biochem. Biophys. Res. Commun. 290 (3): 1030–6. doi:10.1006/bbrc.2001.6288. PMID 11798178.
  16. ↑ Liu TF, Kandala G, Setaluri V (September 2001). "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. doi:10.1074/jbc.M103585200. PMID 11441007.

Further reading

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