Glikoprotein 130
Izvor: Wikipedija
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Interleukin 6 signal transducer (gp130, onkostatin M receptor) | |||||||||||
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Kristalna struktura Gp130 ekstracelularnog domaina (1p9m). | |||||||||||
Dostupne strukture | |||||||||||
1bj8, 1bqu, 1i1r, 1p9m, 1pvh | |||||||||||
Identifikatori | |||||||||||
Simboli | IL6ST; CD130; CDw130; GP130; GP130-RAPS; IL6R-beta | ||||||||||
Vanjski ID | OMIM: 600694 MGI: 96560 HomoloGene: 1645 GeneCards: IL6ST Gene | ||||||||||
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Ortolozi | |||||||||||
Vrsta | Čovek | Miš | |||||||||
Entrez | 3572 | 16195 | |||||||||
Ensembl | ENSG00000134352 | ENSMUSG00000021756 | |||||||||
UniProt | P40189 | Q3TDT5 | |||||||||
RefSeq (mRNA) | NM_002184 | NM_010560 | |||||||||
RefSeq (protein) | NP_002175 | NP_034690 | |||||||||
Lokacija (UCSC) | Chr 5: 55.23 - 55.29 Mb | Chr 13: 113.58 - 113.63 Mb | |||||||||
PubMed pretraga | [1] | [2] |
Glikoprotein 130 (takođe poznat kao gp130, IL6ST, IL6-beta ili CD130) je transmembranski protein. On je osnivački član klase citokinskih receptora. On formira jednu podjedinicu tipa I citokinskih receptora u IL-6 receptorskoj familiji. On se često naziva zajedničkom gp130 podjedinicom, i važan je za signal transdukciju nakon interakcije sa citokinom. Kao i drugi citokinski receptori tipa I, gp130 poseduje WSXWS aminokiselinski motiv koji osigurava korektno proteinsko savijanje i vezivanje liganda. On interaguje sa Janus kinazom da bi izazvao intracelularni signal nakon interakcije receptora sa ligandom. Strukturno, gp130 se sastoji od pet fibronektin tip-III domena i jednog imunoglobulinu-sličnog C2-tipa domena na njegovom ekstracelularnom delu.[1][2]
Svi članovi IL-6 receptorske familije formiraju kompleks sa gp130 proteinom, i putem njega prenose signal. Na primer, IL-6 se veže za IL-6 receptor. Kompleks ova dva proteina se onda asocira sa gp130. Taj kompleks od 3 proteina se homodimerizuje da formira heksamerni kompleks koji može da proizvede nizvodne signale.[3] Postoje mnogi drugi proteini koji se asociraju sa gp130, kao što su kardiotrofin 1 (CT-1), inhibitorni faktor leukemije (LIF), cilijarni neurotrofni faktor (CNTF), onkostatin M (OSM), i IL-11.[4] Postoji takođe nekoliko drugih proteina koji imaju strukturnu sličnost sa gp130, sadrže WSXWS motiv i očuvane cisteinske ostatke. Članovi ove grupe su: LIF-R, OSM-R, i G-CSF-R.
gp130 je važan deo mnogih različitih tipova signalnih kompleksa. Inaktivacija gp130 proteina je letalna kod miševa.[5] Homozigotni miševi nakon rođenja ispoljavaju brojne defekte, jedan od kojih je poremećeni razvoj ventrikularnih miokardijuma. Hematopoetski efekti obuhvataju redukovanje brojeva stem ćelija u slezini i jetri.
gp130 nema unutrašnju tirozin kinaznu aktivnost. Umesto toga, on je fosforilisan na tirozin ostacima nakon kompleksiranja sa drugim proteinima. Fosforilacija dovodi do asocijacije sa JAK/Tyk tirozin kinazama i STAT proteinskim transkripcionim faktorima[6] Specifično, STAT-3 se aktivira, što dovodi do aktivacije mnogih nizvodnih gena. Drugi putevi aktivacije su RAS i MAPK signalizacija.
Za glikoprotein 130 je bilo pokazano interaguje sa TLE1,[7] SOCS3,[8] HER2/neu,[9] PTPN11,[8][10][11] Leukemijski inhibitorni faktor receptorom,[12][13] Grb2,[14] Janus kinaza 1[15][11][16] i SHC1.[17]
- ↑ Hibi et al.; Murakami, M; Saito, M; Hirano, T; Taga, T; Kishimoto, T (1990). „Molecular cloning and expression of an IL-6 signal transducer, gp130”. Cell 63 (6): 1149–1157. DOI:10.1016/0092-8674(90)90411-7. PMID 2261637.
- ↑ Bravo et al.; Staunton, D; Heath, JK; Jones, EY (1998). „Crystal structure of a cytokine-binding region of gp130”. EMBO J 17 (6): 1665–1674. DOI:10.1093/emboj/17.6.1665. PMC 1170514. PMID 9501088.
- ↑ Murakami M, Hibi M, Nakagawa N, Nakagawa T, Yasukawa K, Yamanishi K, Taga T, Kishimoto T (1993). „IL-6-induced homodimerization of gp130 and associated activation of a tyrosine kinase”. Science 260 (5115): 1808–1810. DOI:10.1126/science.8511589. PMID 8511589.
- ↑ Kishimoto T, Akira S, Narazaki M, Taga T (1995). „Interleukin-6 family of cytokines and gp130”. Blood 86 (4): 1243–1254. PMID 7632928.
- ↑ Yoshida K, Taga T, Saito M, Suematsu S, Kumanogoh A, Tanaka T, Fujiwara H, Hirata M, Yamagami T, Nakahata T, Hirabayashi T, Yoneda Y, Tanaka K, Wang W-Z, Mori C, Shiota K, Yoshida N, Kishimoto T (1996). „Targeted disruption of gp130, a common signal transducer for IL-6-family of cytokines, leads to myocardial and hematological disorders”. Proc Natl Acad Sci 93 (1): 407–411. DOI:10.1073/pnas.93.1.407. PMC 40247. PMID 8552649.
- ↑ Kishimoto T, Taga T, Akira S (1994). „Cytokine signal transduction”. Cell 76 (2): 253–262. DOI:10.1016/0092-8674(94)90333-6. PMID 8293462.
- ↑ Liu, Fei; Liu Yin, Li Demin, Zhu Yong, Ouyang Weiming, Xie Xin, Jin Boquan (March 2002). „The transcription co-repressor TLE1 interacted with the intracellular region of gpl30 through its Q domain”. Mol. Cell. Biochem. (Netherlands) 232 (1-2): 163–7. DOI:10.1023/A:1014880813692. ISSN 0300-8177. PMID 12030375.
- ↑ 8,0 8,1 Lehmann, Ute; Schmitz Jochen, Weissenbach Manuela, Sobota Radoslaw M, Hortner Michael, Friederichs Kerstin, Behrmann Iris, Tsiaris William, Sasaki Atsuo, Schneider-Mergener Jens, Yoshimura Akihiko, Neel Benjamin G, Heinrich Peter C, Schaper Fred (January 2003). „SHP2 and SOCS3 contribute to Tyr-759-dependent attenuation of interleukin-6 signaling through gp130”. J. Biol. Chem. (United States) 278 (1): 661–71. DOI:10.1074/jbc.M210552200. ISSN 0021-9258. PMID 12403768.
- ↑ Grant, Susan L; Hammacher Annet, Douglas Andrea M, Goss Geraldine A, Mansfield Rachel K, Heath John K, Begley C Glenn (January 2002). „An unexpected biochemical and functional interaction between gp130 and the EGF receptor family in breast cancer cells”. Oncogene (England) 21 (3): 460–74. DOI:10.1038/sj.onc.1205100. ISSN 0950-9232. PMID 11821958.
- ↑ Anhuf, D; Weissenbach M, Schmitz J, Sobota R, Hermanns H M, Radtke S, Linnemann S, Behrmann I, Heinrich P C, Schaper F (September 2000). „Signal transduction of IL-6, leukemia-inhibitory factor, and oncostatin M: structural receptor requirements for signal attenuation”. J. Immunol. (UNITED STATES) 165 (5): 2535–43. ISSN 0022-1767. PMID 10946280.
- ↑ 11,0 11,1 Kim, H; Baumann H (December 1997). „Transmembrane domain of gp130 contributes to intracellular signal transduction in hepatic cells”. J. Biol. Chem. (UNITED STATES) 272 (49): 30741–7. DOI:10.1074/jbc.272.49.30741. ISSN 0021-9258. PMID 9388212.
- ↑ Timmermann, Andreas; Küster Andrea, Kurth Ingo, Heinrich Peter C, Müller-Newen Gerhard (June 2002). „A functional role of the membrane-proximal extracellular domains of the signal transducer gp130 in heterodimerization with the leukemia inhibitory factor receptor”. Eur. J. Biochem. (Germany) 269 (11): 2716–26. DOI:10.1046/j.1432-1033.2002.02941.x. ISSN 0014-2956. PMID 12047380.
- ↑ Mosley, B; De Imus C, Friend D, Boiani N, Thoma B, Park L S, Cosman D (December 1996). „Dual oncostatin M (OSM) receptors. Cloning and characterization of an alternative signaling subunit conferring OSM-specific receptor activation”. J. Biol. Chem. (UNITED STATES) 271 (51): 32635–43. DOI:10.1074/jbc.271.51.32635. ISSN 0021-9258. PMID 8999038.
- ↑ Lee, I S; Liu Y, Narazaki M, Hibi M, Kishimoto T, Taga T (January 1997). „Vav is associated with signal transducing molecules gp130, Grb2 and Erk2, and is tyrosine phosphorylated in response to interleukin-6”. FEBS Lett. (NETHERLANDS) 401 (2-3): 133–7. DOI:10.1016/S0014-5793(96)01456-1. ISSN 0014-5793. PMID 9013873.
- ↑ Haan, C; Is'harc H, Hermanns H M, Schmitz-Van De Leur H, Kerr I M, Heinrich P C, Grötzinger J, Behrmann I (October 2001). „Mapping of a region within the N terminus of Jak1 involved in cytokine receptor interaction”. J. Biol. Chem. (United States) 276 (40): 37451–8. DOI:10.1074/jbc.M106135200. ISSN 0021-9258. PMID 11468294.
- ↑ Haan, Claude; Heinrich Peter C, Behrmann Iris (January 2002). „Structural requirements of the interleukin-6 signal transducer gp130 for its interaction with Janus kinase 1: the receptor is crucial for kinase activation”. Biochem. J. (England) 361 (Pt 1): 105–11. DOI:10.1042/0264-6021:3610105. ISSN 0264-6021. PMC 1222284. PMID 11742534.
- ↑ Giordano, V; De Falco G, Chiari R, Quinto I, Pelicci P G, Bartholomew L, Delmastro P, Gadina M, Scala G (May 1997). „Shc mediates IL-6 signaling by interacting with gp130 and Jak2 kinase”. J. Immunol. (UNITED STATES) 158 (9): 4097–103. ISSN 0022-1767. PMID 9126968.
- Ip NY, Nye SH, Boulton TG, et al. (1992). „CNTF and LIF act on neuronal cells via shared signaling pathways that involve the IL-6 signal transducing receptor component gp130.”. Cell 69 (7): 1121–32. DOI:10.1016/0092-8674(92)90634-O. PMID 1617725.
- Hibi M, Murakami M, Saito M, et al. (1991). „Molecular cloning and expression of an IL-6 signal transducer, gp130.”. Cell 63 (6): 1149–57. DOI:10.1016/0092-8674(90)90411-7. PMID 2261637.
- Taga T, Hibi M, Hirata Y, et al. (1989). „Interleukin-6 triggers the association of its receptor with a possible signal transducer, gp130.”. Cell 58 (3): 573–81. DOI:10.1016/0092-8674(89)90438-8. PMID 2788034.
- Rodriguez C, Grosgeorge J, Nguyen VC, et al. (1995). „Human gp130 transducer chain gene (IL6ST) is localized to chromosome band 5q11 and possesses a pseudogene on chromosome band 17p11.”. Cytogenet. Cell Genet. 70 (1-2): 64–7. DOI:10.1159/000133993. PMID 7736792.
- Narazaki M, Yasukawa K, Saito T, et al. (1993). „Soluble forms of the interleukin-6 signal-transducing receptor component gp130 in human serum possessing a potential to inhibit signals through membrane-anchored gp130.”. Blood 82 (4): 1120–6. PMID 8353278.
- Davis S, Aldrich TH, Stahl N, et al. (1993). „LIFR beta and gp130 as heterodimerizing signal transducers of the tripartite CNTF receptor.”. Science 260 (5115): 1805–8. DOI:10.1126/science.8390097. PMID 8390097.
- Murakami M, Hibi M, Nakagawa N, et al. (1993). „IL-6-induced homodimerization of gp130 and associated activation of a tyrosine kinase.”. Science 260 (5115): 1808–10. DOI:10.1126/science.8511589. PMID 8511589.
- Sharkey AM, Dellow K, Blayney M, et al. (1996). „Stage-specific expression of cytokine and receptor messenger ribonucleic acids in human preimplantation embryos.”. Biol. Reprod. 53 (4): 974–81. DOI:10.1095/biolreprod53.4.974. PMID 8547494.
- Mosley B, De Imus C, Friend D, et al. (1997). „Dual oncostatin M (OSM) receptors. Cloning and characterization of an alternative signaling subunit conferring OSM-specific receptor activation.”. J. Biol. Chem. 271 (51): 32635–43. DOI:10.1074/jbc.271.51.32635. PMID 8999038.
- Lee IS, Liu Y, Narazaki M, et al. (1997). „Vav is associated with signal transducing molecules gp130, Grb2 and Erk2, and is tyrosine phosphorylated in response to interleukin-6.”. FEBS Lett. 401 (2-3): 133–7. DOI:10.1016/S0014-5793(96)01456-1. PMID 9013873.
- Auguste P, Guillet C, Fourcin M, et al. (1997). „Signaling of type II oncostatin M receptor.”. J. Biol. Chem. 272 (25): 15760–4. DOI:10.1074/jbc.272.25.15760. PMID 9188471.
- Schiemann WP, Bartoe JL, Nathanson NM (1997). „Box 3-independent signaling mechanisms are involved in leukemia inhibitory factor receptor alpha- and gp130-mediated stimulation of mitogen-activated protein kinase. Evidence for participation of multiple signaling pathways which converge at Ras.”. J. Biol. Chem. 272 (26): 16631–6. DOI:10.1074/jbc.272.26.16631. PMID 9195977.
- Diamant M, Rieneck K, Mechti N, et al. (1997). „Cloning and expression of an alternatively spliced mRNA encoding a soluble form of the human interleukin-6 signal transducer gp130.”. FEBS Lett. 412 (2): 379–84. DOI:10.1016/S0014-5793(97)00750-3. PMID 9256256.
- Koshelnick Y, Ehart M, Hufnagl P, et al. (1997). „Urokinase receptor is associated with the components of the JAK1/STAT1 signaling pathway and leads to activation of this pathway upon receptor clustering in the human kidney epithelial tumor cell line TCL-598.”. J. Biol. Chem. 272 (45): 28563–7. DOI:10.1074/jbc.272.45.28563. PMID 9353320.
- Kim H, Baumann H (1998). „Transmembrane domain of gp130 contributes to intracellular signal transduction in hepatic cells.”. J. Biol. Chem. 272 (49): 30741–7. DOI:10.1074/jbc.272.49.30741. PMID 9388212.
- Bravo J, Staunton D, Heath JK, Jones EY (1998). „Crystal structure of a cytokine-binding region of gp130.”. EMBO J. 17 (6): 1665–74. DOI:10.1093/emboj/17.6.1665. PMC 1170514. PMID 9501088.
- Barton VA, Hudson KR, Heath JK (1999). „Identification of three distinct receptor binding sites of murine interleukin-11.”. J. Biol. Chem. 274 (9): 5755–61. DOI:10.1074/jbc.274.9.5755. PMID 10026196.
- Hirota H, Chen J, Betz UA, et al. (1999). „Loss of a gp130 cardiac muscle cell survival pathway is a critical event in the onset of heart failure during biomechanical stress.”. Cell 97 (2): 189–98. DOI:10.1016/S0092-8674(00)80729-1. PMID 10219240.
- Tacken I, Dahmen H, Boisteau O, et al. (1999). „Definition of receptor binding sites on human interleukin-11 by molecular modeling-guided mutagenesis.”. Eur. J. Biochem. 265 (2): 645–55. DOI:10.1046/j.1432-1327.1999.00755.x. PMID 10504396.
- Chung TD, Yu JJ, Kong TA, et al. (2000). „Interleukin-6 activates phosphatidylinositol-3 kinase, which inhibits apoptosis in human prostate cancer cell lines.”. Prostate 42 (1): 1–7. DOI:10.1002/(SICI)1097-0045(20000101)42:1<1::AID-PROS1>3.0.CO;2-Y. PMID 10579793.
PDB Galerija | ||||||||||||
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1-50 | CD1 (a-c, 1A, 1D, 1E) • CD2 • CD3 (γ, δ, ε) • CD4 • CD5 • CD6 • CD7 • CD8 (a) • CD9 • CD10 • CD11 (a, b, c) • CD13 • CD14 • CD15 • CD16 (A, B) • CD18 • CD19 • CD20 • CD21 • CD22 • CD23 • CD24 • CD25 • CD26 • CD27 • CD28 • CD29 • CD30 • CD31 • CD32 (A, B) • CD33 • CD34 • CD35 • CD36 • CD37 • CD38 • CD39 • CD40 • CD41 • CD42 (a, b, c, d) • CD43 • CD44 • CD45 • CD46 • CD47 • CD48 • CD49 (a, b, c, d, e, f) • CD50 |
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51-100 | CD51 • CD52 • CD53 • CD54 • CD55 • CD56 • CD57 • CD58 • CD59 • CD61 • CD62 (E, L, P) • CD63 • CD64 (A, B, C) • CD66 (a, b, c, d, e, f) • CD68 • CD69 • CD70 • CD71 • CD72 • CD73 • CD74 • CD78 • CD79 (a, b) • CD80 • CD81 • CD82 • CD83 • CD84 • CD85 (a, d, e, h, j, k) • CD86 • CD87 • CD88 • CD89 • CD90 • CD91- CD92 • CD93 • CD94 • CD95 • CD96 • CD97 • CD98 • CD99 • CD100 |
101-150 | CD101 • CD102 • CD103 • CD104 • CD105 • CD106 • CD107 (a, b) • CD108 • CD109 • CD110 • CD111 • CD112 • CD113 • CD114 • CD115 • CD116 • CD117 • CD118 • CD119 • CD120 (a, b) • CD121 (a, b) • CD122 • CD123 • CD124 • CD125 • CD126 • CD127 • CD129 • CD130 • CD131 • CD132 • CD133 • CD134 • CD135 • CD136 • CD137 • CD138 • CD140b • CD141 • CD142 • CD143 • CD144 • CD146 • CD147 • CD148 • CD150 |
151-200 | CD151 • CD152 • CD153 • CD154 • CD155 • CD156 (a, b, c) • CD157 • CD158 (a, d, e, i, k) • CD159 (a, c) • CD160 • CD161 • CD162 • CD163 • CD164 • CD166 • CD167 (a, b) • CD168 • CD169 • CD170 • CD171 • CD172 (a, b, g) • CD174 • CD177 • CD178 • CD179 (a, b) • CD181 • CD182 • CD183 • CD184 • CD185 • CD186 • CD191 • CD192 • CD193 • CD194 • CD195 • CD196 • CD197 • CDw198 • CDw199 • CD200 |
201-250 | CD201 • CD202b • CD204 • CD205 • CD206 • CD207 • CD208 • CD209 • CDw210 (a, b) • CD212 • CD213a (1, 2) • CD217 • CD218 (a, b) • CD220 • CD221 • CD222 • CD223 • CD224 • CD225 • CD226 • CD227 • CD228 • CD229 • CD230 • CD233 • CD234 • CD235 (a, b) • CD236 • CD238 • CD239 • CD240CE • CD241 • CD243 • CD244 • CD246 • CD247- CD248 • CD249 |
251-300 | CD252 • CD253 • CD254 • CD256 • CD257 • CD258 • CD261 • CD262 • CD264 • CD265 • CD266 • CD267 • CD268 • CD269 • CD271 • CD272 • CD273 • CD274 • CD275 • CD276 • CD278 • CD279 • CD280 • CD281 • CD282 • CD283 • CD284 • CD286 • CD288 • CD289 • CD290 • CD292 • CDw293 • CD294 • CD295 • CD297 • CD298 • CD299 |
301-350 |
Receptori za antitela: Fc receptor |
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Receptori za antigene |
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Citokinski receptor | Pogledajte citokinski receptori | ||||||||||||||||||
Receptori ćelija ubica slični IG | KIR2DL1, KIR2DL2, KIR2DL3, KIR2DL4, KIR2DL5A, KIR2DL5B, KIR2DS1, KIR2DS2, KIR2DS3, KIR2DS4, KIR2DS5, KIR3DL1, KIR3DL2, KIR3DL3, KIR3DS1 | ||||||||||||||||||
Leukocitni receptori slični IG | LILRA1 • LILRA2 • LILRA3 • LILRA4 • LILRA5 • LILRA6 • LILRB1 • LILRB2 • LILRB3 • LILRB4 • LILRB5 • LILRA6 • LILRA5 | ||||||||||||||||||
B trdu: peptidi (nrpl/grfl/cytl/horl), receptori (lgic, enzr, gprc, igsr, intg, nrpr/grfr/cytr), itra (adap, gbpr, mapk), calc, lipd, signalni putevi (hedp, wntp, tgfp+mapp, notp, jakp, fsap, hipp, tlrp) |
Hemokinski receptor (GPCR) |
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TNF receptor |
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JAK-STAT |
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Ig superfamilija | |||||||
S/T | TGF-beta (1, 2) | ||||||
Drugi | IL-17 (IL17RA, IL17RB, IL17RC, IL17RD, IL17RE) | ||||||
Po familiji |
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Drugi | |||||||||||||||||||||||||||||||||||||||||||
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Mukoproteini |
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Drugi | Aktivin i inhibin • ADAM • Alfa 1-antihimotripsin • Apolipoprotein H • CD70 • Asijaloglikoprotein • Avidin • B-ćelijski aktivacioni faktor • 4-1BB ligand • Kolesterilester transfer protein • Klasterin • Faktor stimulacije kolonije • Hemopeksin • Laktoferin • Membranski glikoproteini • Mijelin protein nula • Osteonektin • Protein C • Protein S • Proteoglikan • Serum amiloid P komponenta • Sialoglikoprotein (CD43, Glikoforin, Glikoforin C) • Trombopoetin • Tiroglobulin • Tiroksin-vezujući proteini • Transkortin • Faktor nekroze tumora-alfa • Uteroglobin • Vitronektin | ||||
Biohemijske familije: Ugljeni hidrati (Glikozidi,Alkoholi) • Lipidi (Steroidi,Fosfolipidi,Glikolipidi,Masne kiseline,Tetrapiroli) • Proteini (Aminokiseline,Peptidi,Glikoproteini) • Nukleobaze/Nukleinske kiseline |
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