Receptor insulinu sličnog faktora rasta 1

edit
Receptor insulinu sličnog faktora rasta 1‎‎

Prva tri domena receptora insulinu sličnog faktora rasta 1‎‎. PDB prikaz baziran na 1igr.
Dostupne strukture
1IGR, 1JQH, 1K3A, 1M7N, 1P4O, 2OJ9, 2ZM3, 3D94, 3F5P, 3I81, 3LVP, 3LW0, 3NW5, 3NW6, 3NW7, 3O23, 3QQU
Identifikatori
SimboliIGF1R; CD221; IGFIR; IGFR; JTK13
Vanjski IDOMIM: 147370 MGI: 96433 HomoloGene: 30997 GeneCards: IGF1R Gene
EC broj2.7.10.1
Ontologija gena
Molekularna funkcija aktivnost proteinske tirozinske kinaze
aktivnost receptora insulinu sličnog faktora rasta
vezivanje insulinskog receptora
Celularna komponenta integralno sa ćelijskom membranom
kaveola
membrana
Biološki proces imunski respons
prenos signala
aksonogeneza
Pregled RNK izražavanja
podaci
Ortolozi
VrstaČovekMiš
Entrez348016001
EnsemblENSG00000140443ENSMUSG00000005533
UniProtP08069Q60751
RefSeq (mRNA)NM_000875.3NM_010513.2
RefSeq (protein)NP_000866.1NP_034643.2
Lokacija (UCSC)Chr 15:
99.19 - 99.51 Mb
Chr 7:
67.95 - 68.23 Mb
PubMed pretraga[1][2]

Receptor insulinu sličnog faktora rasta 1 je protein koji je prisutan na površini ljudskih ćelija. On je transmembranski receptor koji se aktivira IGF-1 hormonom (insulinu sličan faktor rasta 1) i srodnim hormonom IGF-2. On pripada velikoj klasi tirozinsko kinaznih receptora . Ovaj receptor posreduje dejstvo IGF-1, koji je polipeptidni proteinski hormon sličan insulinu. IGF-1 utiče na razviće i nastavlja da vrši anaboličko dejstvo kod odraslih. On može da indukuje hipertroifju skeletalnih mišića i drugih ciljnih tkiva. Miševi bez IGF-1 receptora umiru u kasnijem periodu razvića, i manifestuju dramatičnu redukcu telesne mase, što potvrđuje jak uticaj ovog receptora. Miševi sa samo jednom funkcionalnom kopijom IGF1R su normalni, ali ispoljavaju ~15% umanjenje telesne mase.

Interakcije

Receptor insulinu sličnog faktora rasta 1 formira interakcije sa SOCS3,[1] PTPN11,[2][3] SOCS2,[4] GRB10,[5][6][7][8] PIK3R3,[9] C-src tirosinska kinaza,[10] EHD1,[11] Cbl genom,[12] RAS p21 proteinskim aktivatorom 1,[3] IRS1,[2][6][13] ARHGEF12,[14] YWHAE,[15] Mdm2,[12] SHC1[6][13][16] i NEDD4.[5][12]

Regulacija

Postoji evidencija da je IGF1R negativno regulisan dejstvom mikroRNK miR-7.[17]

References

  1. Dey, B R; Furlanetto R W, Nissley P (November 2000). „Suppressor of cytokine signaling (SOCS)-3 protein interacts with the insulin-like growth factor-I receptor”. Biochem. Biophys. Res. Commun. (UNITED STATES) 278 (1): 38–43. DOI:10.1006/bbrc.2000.3762. ISSN 0006-291X. PMID 11071852. 
  2. 2,0 2,1 Mañes, S; Mira E, Gómez-Mouton C, Zhao Z J, Lacalle R A, Martínez-A C (April 1999). „Concerted activity of tyrosine phosphatase SHP-2 and focal adhesion kinase in regulation of cell motility”. Mol. Cell. Biol. (UNITED STATES) 19 (4): 3125–35. ISSN 0270-7306. PMC 84106. PMID 10082579. 
  3. 3,0 3,1 Seely, B L; Reichart D R, Staubs P A, Jhun B H, Hsu D, Maegawa H, Milarski K L, Saltiel A R, Olefsky J M (August 1995). „Localization of the insulin-like growth factor I receptor binding sites for the SH2 domain proteins p85, Syp, and GTPase activating protein”. J. Biol. Chem. (UNITED STATES) 270 (32): 19151–7. DOI:10.1074/jbc.270.32.19151. ISSN 0021-9258. PMID 7642582. 
  4. Dey, B R; Spence S L, Nissley P, Furlanetto R W (September 1998). „Interaction of human suppressor of cytokine signaling (SOCS)-2 with the insulin-like growth factor-I receptor”. J. Biol. Chem. (UNITED STATES) 273 (37): 24095–101. DOI:10.1074/jbc.273.37.24095. ISSN 0021-9258. PMID 9727029. 
  5. 5,0 5,1 Vecchione, Andrea; Marchese Adriano, Henry Pauline, Rotin Daniela, Morrione Andrea (May 2003). „The Grb10/Nedd4 complex regulates ligand-induced ubiquitination and stability of the insulin-like growth factor I receptor”. Mol. Cell. Biol. (United States) 23 (9): 3363–72. DOI:10.1128/MCB.23.9.3363-3372.2003. ISSN 0270-7306. PMC 153198. PMID 12697834. 
  6. 6,0 6,1 6,2 Dey, B R; Frick K, Lopaczynski W, Nissley S P, Furlanetto R W (June 1996). „Evidence for the direct interaction of the insulin-like growth factor I receptor with IRS-1, Shc, and Grb10”. Mol. Endocrinol. (UNITED STATES) 10 (6): 631–41. DOI:10.1210/me.10.6.631. ISSN 0888-8809. PMID 8776723. 
  7. He, W; Rose D W, Olefsky J M, Gustafson T A (March 1998). „Grb10 interacts differentially with the insulin receptor, insulin-like growth factor I receptor, and epidermal growth factor receptor via the Grb10 Src homology 2 (SH2) domain and a second novel domain located between the pleckstrin homology and SH2 domains”. J. Biol. Chem. (UNITED STATES) 273 (12): 6860–7. DOI:10.1074/jbc.273.12.6860. ISSN 0021-9258. PMID 9506989. 
  8. Morrione, A; Valentinis B, Li S, Ooi J Y, Margolis B, Baserga R (July 1996). „Grb10: A new substrate of the insulin-like growth factor I receptor”. Cancer Res. (UNITED STATES) 56 (14): 3165–7. ISSN 0008-5472. PMID 8764099. 
  9. Mothe, I; Delahaye L, Filloux C, Pons S, White M F, Van Obberghen E (December 1997). „Interaction of wild type and dominant-negative p55PIK regulatory subunit of phosphatidylinositol 3-kinase with insulin-like growth factor-1 signaling proteins”. Mol. Endocrinol. (UNITED STATES) 11 (13): 1911–23. DOI:10.1210/me.11.13.1911. ISSN 0888-8809. PMID 9415396. 
  10. Arbet-Engels, C; Tartare-Deckert S, Eckhart W (February 1999). „C-terminal Src kinase associates with ligand-stimulated insulin-like growth factor-I receptor”. J. Biol. Chem. (UNITED STATES) 274 (9): 5422–8. DOI:10.1074/jbc.274.9.5422. ISSN 0021-9258. PMID 10026153. 
  11. Rotem-Yehudar, R; Galperin E, Horowitz M (August 2001). „Association of insulin-like growth factor 1 receptor with EHD1 and SNAP29”. J. Biol. Chem. (United States) 276 (35): 33054–60. DOI:10.1074/jbc.M009913200. ISSN 0021-9258. PMID 11423532. 
  12. 12,0 12,1 12,2 Sehat, Bita; Andersson Sandra, Girnita Leonard, Larsson Olle (July 2008). „Identification of c-Cbl as a new ligase for insulin-like growth factor-I receptor with distinct roles from Mdm2 in receptor ubiquitination and endocytosis”. Cancer Res. (United States) 68 (14): 5669–77. DOI:10.1158/0008-5472.CAN-07-6364. PMID 18632619. 
  13. 13,0 13,1 Tartare-Deckert, S; Sawka-Verhelle D, Murdaca J, Van Obberghen E (October 1995). „Evidence for a differential interaction of SHC and the insulin receptor substrate-1 (IRS-1) with the insulin-like growth factor-I (IGF-I) receptor in the yeast two-hybrid system”. J. Biol. Chem. (UNITED STATES) 270 (40): 23456–60. DOI:10.1074/jbc.270.40.23456. ISSN 0021-9258. PMID 7559507. 
  14. Taya, S; Inagaki N, Sengiku H, Makino H, Iwamatsu A, Urakawa I, Nagao K, Kataoka S, Kaibuchi K (November 2001). „Direct interaction of insulin-like growth factor-1 receptor with leukemia-associated RhoGEF”. J. Cell Biol. (United States) 155 (5): 809–20. DOI:10.1083/jcb.200106139. ISSN 0021-9525. PMC 2150867. PMID 11724822. 
  15. Craparo, A; Freund R, Gustafson T A (April 1997). „14-3-3 (epsilon) interacts with the insulin-like growth factor I receptor and insulin receptor substrate I in a phosphoserine-dependent manner”. J. Biol. Chem. (UNITED STATES) 272 (17): 11663–9. DOI:10.1074/jbc.272.17.11663. ISSN 0021-9258. PMID 9111084. 
  16. Santen, R J; Song R X, Zhang Z, Kumar R, Jeng M-H, Masamura A, Lawrence J, Berstein L, Yue W (July 2005). „Long-term estradiol deprivation in breast cancer cells up-regulates growth factor signaling and enhances estrogen sensitivity”. Endocr. Relat. Cancer. 12 (England) Suppl 1 (Supplement_1): S61–73. DOI:10.1677/erc.1.01018. ISSN 1351-0088. PMID 16113100. 
  17. Jiang, Lu; Liu, Xiqiang; Chen, Zujian; Jin, Yi; Heidbreder, Caroline E.; Kolokythas, Antonia; Wang, Anxun; Dai, Yang i dr.. (2010). „MicroRNA-7 targets IGF1R (insulin-like growth factor 1 receptor) in tongue squamous cell carcinoma cells”. Biochemical Journal 432 (1): 199–205. DOI:10.1042/BJ20100859. PMID 20819078. 

Literatura

  • Benito M, Valverde AM, Lorenzo M (1996). „IGF-I: a mitogen also involved in differentiation processes in mammalian cells.”. Int. J. Biochem. Cell Biol. 28 (5): 499–510. DOI:10.1016/1357-2725(95)00168-9. PMID 8697095. 
  • Butler AA, Yakar S, Gewolb IH, et al. (1999). „Insulin-like growth factor-I receptor signal transduction: at the interface between physiology and cell biology.”. Comp. Biochem. Physiol. B, Biochem. Mol. Biol. 121 (1): 19–26. DOI:10.1016/S0305-0491(98)10106-2. PMID 9972281. 
  • Zhang X, Yee D (2001). „Tyrosine kinase signalling in breast cancer: insulin-like growth factors and their receptors in breast cancer.”. Breast Cancer Res. 2 (3): 170–5. DOI:10.1186/bcr50. PMC 138771. PMID 11250706. 
  • Gross JM, Yee D (2004). „The type-1 insulin-like growth factor receptor tyrosine kinase and breast cancer: biology and therapeutic relevance.”. Cancer Metastasis Rev. 22 (4): 327–36. DOI:10.1023/A:1023720928680. PMID 12884909. 
  • Adams TE, McKern NM, Ward CW (2005). „Signalling by the type 1 insulin-like growth factor receptor: interplay with the epidermal growth factor receptor.”. Growth Factors 22 (2): 89–95. DOI:10.1080/08977190410001700998. PMID 15253384. 
  • Surmacz E, Bartucci M (2005). „Role of estrogen receptor alpha in modulating IGF-I receptor signaling and function in breast cancer.”. J. Exp. Clin. Cancer Res. 23 (3): 385–94. PMID 15595626. 
  • Wood AW, Duan C, Bern HA (2005). „Insulin-like growth factor signaling in fish.”. Int. Rev. Cytol. 243: 215–85. DOI:10.1016/S0074-7696(05)43004-1. PMID 15797461. 
  • Sarfstein R, Maor S, Reizner N, et al. (2006). „Transcriptional regulation of the insulin-like growth factor-I receptor gene in breast cancer.”. Mol. Cell. Endocrinol. 252 (1-2): 241–6. DOI:10.1016/j.mce.2006.03.018. PMID 16647191. 

Vidi još

Spoljašnje veze

  • p
  • r
  • u
PDB Galerija
1igr: Receptor tipa 1 insulinu sličnog faktora rasta (domeni 1-3)
1igr: Receptor tipa 1 insulinu sličnog faktora rasta (domeni 1-3)  
1jqh: Kinazni domen IGF-1 receptora
1jqh: Kinazni domen IGF-1 receptora  
1k3a: Struktura receptora insulin sličnog faktora rasta 1
1k3a: Struktura receptora insulin sličnog faktora rasta 1  
1m7n: Struktura neaktiviranog kinaznog domena receptora insulinu sličnog faktora rasta
1m7n: Struktura neaktiviranog kinaznog domena receptora insulinu sličnog faktora rasta  
1p4o: Struktura neaktiviranog IGF-1R kinaznog domena
1p4o: Struktura neaktiviranog IGF-1R kinaznog domena  
2oj9: Struktura IGF-1R kinazni domen u kompleksu sa benzimidazolskim inhibitorom
2oj9: Struktura IGF-1R kinazni domen u kompleksu sa benzimidazolskim inhibitorom  
  • p
  • r
  • u
  • p
  • r
  • u
Receptori faktora rasta
EGFR • ERBB2 • ERBB3 • ERBB4
IGF1R • INSR • INSRR
CSF1R • FLT3 • KIT • PDGFR (PDGFRA, PDGFRB)
FGFR1 • FGFR2 • FGFR3 • FGFR4
VEGFR1 • VEGFR2 • VEGFR3 • VEGFR4
MET • RON
NTRK1 • NTRK2 • NTRK3
EPH receptorska familija
EPHA1 • EPHA2 • EPHA3 • EPHA4 • EPHA5 • EPHA6 • EPHA7 • EPHA8 • EPHB1 • EPHB2 • EPHB3 • EPHB4 • EPHB5 • EPHB6 • EPHX
LTK receptorska familija
LTK • ALK
TIE receptorska familija
TIE • TEK
ROR receptorska familija
ROR1 • ROR2
DDR receptorska familija
DDR1 • DDR2
PTK7 receptorska familija
RYK receptorska familija
MuSK receptorska familija
ROS receptorska familija
ROS1
AATYK receptorska familija
AATYK • AATYK2 • AATYK3
AXL receptorska familija
AXL • MER • TYRO3
RET receptorska familija
nekategorisani
  • p
  • r
  • u
ABL familija
ABL1 • ARG
ACK familija
ACK1 • TNK1
CSK familija
CSK • MATK
FAK familija
FAK • PYK2
FES familija
FES • FER
FRK familija
FRK • BRK • SRMS
JAK familija
JAK1 • JAK2 • JAK3 • TYK2
SRC-A familija
SRC • FGR • FYN • YES1
SRC-B familija
BLK • HCK • LCK • LYN
TEC familija
TEC • BMX • BTK • ITK • TXK
SYK familija
SYK • ZAP70
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
  • p
  • r
  • u
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
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
CD300A • CD301 • CD302 • CD303 • CD304 • CD305 • CD306 • CD307 • CD309 • CD312 • CD314 • CD315 • CD316 • CD317 • CD318 • CD320 • CD321 • CD322 • CD324 • CD325 • CD326 • CD328 • CD329 • CD331 • CD332 • CD333 • CD334 • CD335 • CD336 • CD337 • CD338 • CD339 • CD340 • CD344 • CD349 • CD350
  • p
  • r
  • u
Nervni faktori rasta
niski afinitet/p75 - visok afinitet Trk (TrkA, TrkB, TrkC) - Cilijarni neurotrofni faktor
Somatomedin
Insulinu-sličan faktor rasta 1 - Insulinu-sličan faktor rasta 2
CSF
Stem ćelijski faktor - Eritropoietin
TGF put
TGF-beta (1, 2) - Aktivin (1, 2) - Bone morfogenetski protein (1, 2)
Drugi
vidi isto Faktori rasta
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)
  • p
  • r
  • u
Teme
Tipovi
EC1 Oksidoreduktaze/spisak  • EC2 Transferaze/spisak  • EC3 Hidrolaze/spisak  • EC4 Lijaze/spisak  • EC5 Izomeraze/spisak  • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6