GIPC1
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GIPC1 (GIPC familija koja sadrži PDZ domen, član 1) je protein koji je kod ljudi kodiran GIPC1 genom.[1][2][3]
Interakcije
urediGIPC1 formira interakcije sa Beta-1 adrenergičkim receptorom,[4] ITGA5,[5] ITGA6,[5] TPBG,[6] RGS19,[7] TYRP1,[8] GLUT1,[9] Aktinin, alfa 1,[9] KIF1B,[9] LRP2,[10][11][12] LHCGR,[13] LRP1[10] i MYO6.[14][15]
Reference
uredi- ↑ 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.
- ↑ 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.
- ↑ „Entrez Gene: GIPC1 GIPC PDZ domain containing family, member 1”.
- ↑ Hu, Liaoyuan A; Chen Wei, Martin Negin P, Whalen Erin J, Premont Richard T, Lefkowitz Robert J (July 2003). „GIPC interacts with the beta1-adrenergic receptor and regulates beta1-adrenergic receptor-mediated ERK activation”. J. Biol. Chem. (United States) 278 (28): 26295–301. DOI:10.1074/jbc.M212352200. ISSN 0021-9258. PMID 12724327.
- ↑ 5,0 5,1 Tani, T T; Mercurio A M (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. (United States) 276 (39): 36535–42. DOI:10.1074/jbc.M105785200. ISSN 0021-9258. PMID 11479315.
- ↑ Awan, Abida; Lucic Melinda R, Shaw David M, Sheppard Freda, Westwater Caroline, Lyons Steve A, Stern Peter L (January 2002). „5T4 interacts with TIP-2/GIPC, a PDZ protein, with implications for metastasis”. Biochem. Biophys. Res. Commun. (United States) 290 (3): 1030–6. DOI:10.1006/bbrc.2001.6288. ISSN 0006-291X. PMID 11798178.
- ↑ Lou, X; Yano H, Lee F, Chao M V, Farquhar M G (March 2001). „GIPC and GAIP form a complex with TrkA: a putative link between G protein and receptor tyrosine kinase pathways”. Mol. Biol. Cell (United States) 12 (3): 615–27. ISSN 1059-1524. PMC 30968. PMID 11251075.
- ↑ Liu, T F; 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. (United States) 276 (38): 35768–77. DOI:10.1074/jbc.M103585200. ISSN 0021-9258. PMID 11441007.
- ↑ 9,0 9,1 9,2 Bunn, R C; Jensen M A, Reed B C (April 1999). „Protein interactions with the glucose transporter binding protein GLUT1CBP that provide a link between GLUT1 and the cytoskeleton”. Mol. Biol. Cell (UNITED STATES) 10 (4): 819–32. ISSN 1059-1524. PMC 25204. PMID 10198040.
- ↑ 10,0 10,1 Gotthardt, M; Trommsdorff M, Nevitt M F, Shelton J, Richardson J A, 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. (UNITED STATES) 275 (33): 25616–24. DOI:10.1074/jbc.M000955200. ISSN 0021-9258. PMID 10827173.
- ↑ Petersen, Helle Heibroch; Hilpert Jan, Militz Daniel, Zandler Valerie, Jacobsen Christian, Roebroek Anton J M, Willnow Thomas E (February 2003). „Functional interaction of megalin with the megalinbinding protein (MegBP), a novel tetratrico peptide repeat-containing adaptor molecule”. J. Cell. Sci. (England) 116 (Pt 3): 453–61. DOI:10.1242/jcs.00243. ISSN 0021-9533. PMID 12508107.
- ↑ Lou, Xiaojing; McQuistan Tammie, Orlando Robert A, Farquhar Marilyn Gist (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. (United States) 13 (4): 918–27. ISSN 1046-6673. PMID 11912251.
- ↑ Hirakawa, Takashi; Galet Colette, Kishi Mikiko, Ascoli Mario (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. (United States) 278 (49): 49348–57. DOI:10.1074/jbc.M306557200. ISSN 0021-9258. PMID 14507927.
- ↑ Ewing, Rob M; Chu Peter, Elisma Fred, Li Hongyan, Taylor Paul, Climie Shane, McBroom-Cerajewski Linda, Robinson Mark D, O'Connor Liam, Li Michael, Taylor Rod, Dharsee Moyez, Ho Yuen, Heilbut Adrian, Moore Lynda, Zhang Shudong, Ornatsky Olga, Bukhman Yury V, Ethier Martin, Sheng Yinglun, Vasilescu Julian, Abu-Farha Mohamed, Lambert Jean-Philippe, Duewel Henry S, Stewart Ian I, Kuehl Bonnie, Hogue Kelly, Colwill Karen, Gladwish Katharine, Muskat Brenda, Kinach Robert, Adams Sally-Lin, Moran Michael F, Morin Gregg B, Topaloglou Thodoros, Figeys Daniel (2007). „Large-scale mapping of human protein-protein interactions by mass spectrometry”. Mol. Syst. Biol. (England) 3 (1): 89. DOI:10.1038/msb4100134. PMC 1847948. PMID 17353931.
- ↑ Aschenbrenner, Laura; Lee TinThu, Hasson Tama (July 2003). „Myo6 facilitates the translocation of endocytic vesicles from cell peripheries”. Mol. Biol. Cell (United States) 14 (7): 2728–43. DOI:10.1091/mbc.E02-11-0767. ISSN 1059-1524. PMC 165672. PMID 12857860.
Literatura
uredi- Katoh M (2002). „GIPC gene family (Review).”. Int. J. Mol. Med. 9 (6): 585–9. PMID 12011974.
- Hasson T (2004). „Myosin VI: two distinct roles in endocytosis.”. J. Cell. Sci. 116 (Pt 17): 3453–61. DOI:10.1242/jcs.00669. PMID 12893809.
- Gress TM, Müller-Pillasch F, Geng M, et al. (1996). „A pancreatic cancer-specific expression profile.”. Oncogene 13 (8): 1819–30. PMID 8895530.
- De Vries L, Elenko E, Hubler L, et al. (1997). „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. DOI:10.1073/pnas.93.26.15203. PMC 26381. PMID 8986788.
- Bunn RC, Jensen MA, Reed BC (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. PMC 25204. PMID 10198040.
- Wang LH, Kalb RG, Strittmatter SM (1999). „A PDZ protein regulates the distribution of the transmembrane semaphorin, M-SemF.”. J. Biol. Chem. 274 (20): 14137–46. DOI:10.1074/jbc.274.20.14137. PMID 10318831.
- Cai H, Reed RR (1999). „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. PMID 10414980.
- Gotthardt M, Trommsdorff M, Nevitt MF, et al. (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.
- Gao Y, Li M, Chen W, Simons M (2000). „Synectin, syndecan-4 cytoplasmic domain binding PDZ protein, inhibits cell migration.”. J. Cell. Physiol. 184 (3): 373–9. DOI:10.1002/1097-4652(200009)184:3<373::AID-JCP12>3.0.CO;2-I. PMID 10911369.
- Von Kap-Herr C, Kandala G, Mann SS, et al. (2000). „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. DOI:10.1159/000015621. PMID 10965131.
- Lou X, Yano H, Lee F, et al. (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. PMC 30968. PMID 11251075.
- Liu TF, Kandala G, Setaluri V (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.
- Ligensa T, Krauss S, Demuth D, et al. (2001). „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. DOI:10.1074/jbc.M104509200. PMID 11445579.
- Tani TT, Mercurio AM (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.
- Blobe GC, Liu X, Fang SJ, et al. (2001). „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. DOI:10.1074/jbc.M106831200. PMID 11546783.
- Awan A, Lucic MR, Shaw DM, et al. (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.
- El Mourabit H, Poinat P, Koster J, et al. (2002). „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. DOI:10.1016/S0945-053X(01)00198-6. PMID 11852236.
- Lou X, McQuistan T, Orlando RA, Farquhar MG (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.