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PDGFRB

Izvor: Wikipedija
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Receptor beta-tipa iz trombocida izvedenog faktora rasta

Trakasti prikaz dva molekula ljudskog PDGF receptora beta (žuto i magenta) u kompleksu sa dimerinim PDGF-B .[1]
Dostupne strukture
1GQ5, 1H9O, 1LWP, 1SHA, 2L6W, 2PLD, 2PLE, 3MJG
Identifikatori
SimboliPDGFRB; CD140B; IBGC4; IMF1; JTK12; PDGFR; PDGFR-1; PDGFR1
Vanjski IDOMIM: 173410 MGI: 97531 HomoloGene: 1960 GeneCards: PDGFRB Gene
EC broj2.7.10.1
Pregled RNK izražavanja
podaci
Ortolozi
VrstaČovekMiš
Entrez515918596
EnsemblENSG00000113721ENSMUSG00000024620
UniProtP09619P05622
Ref. Sekv. (iRNK)NM_002609NM_001146268
Ref. Sekv. (protein)NP_002600NP_001139740
Lokacija (UCSC)Chr 5:
149.49 - 149.54 Mb		Chr 18:
61.05 - 61.09 Mb
PubMed pretraga[1][2]

Receptor beta-tipa iz trombocida izvedenog faktora rasta je protein koji je kod ljudi kodiran PDGFRB genom.

Ovaj gen kodira tirozinsko kinazni receptor sa ćelijske površine za članove familije faktora rasta koji su izvedeni iz trombocita. Ti faktori rasta su mitogeni za ćelije mesenhimalnog porekla. Identitet faktora rasta vezanog za receptorski monomer određuje da li je funkcionalni receptor homodimer ili heterodimer, formiran od oba faktora rasta, alfa i beta polipeptida. Ovaj gen je na hromozomu 5 pored gena za receptore granulocitnog makrofagnog faktora stimulacije kolonija i stimulacionog faktor makrophagnih kolonija; sva tri gena učestvuju u 5q- sindrom. Translokacija između hromozoma 5 i 12, kojom se spaja ovaj gen sa translociranim genom leukemije, ETV6, dovodi do hroničnog mijeloproliferativnog poremećaja sa eozinofilijom.[2]

Interakcija

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PDGFRB formira interakcije sa PTPN11,[3][4] NCK1,[5][6] Grb2,[6][7][8] Kaveolin 1,[9] PDGFRA,[10][11] Natrijum-vodonik antiporter 3 regulator 1,[12] RAS p21 protein activator 1,[13][14] CRK,[15] SHC1[16] and NCK2.[6][17][18]

Povezano

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Reference

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  1. ↑ PDB 3MJG; Shima AHR, Liua H, Fociaa PJ, Chena X, Linb PC, He X. (2010). „Structures of a platelet-derived growth factor/propeptide complex and a platelet-derived growth factor/receptor complex”. PNAS 107 (25): 11307–12. DOI:10.1073/pnas.1000806107. PMC 2895058. PMID 20534510. ; rendered using PyMOL.
  2. ↑ „Entrez Gene: PDGFRB platelet-derived growth factor receptor, beta polypeptide”. 
  3. ↑ Keilhack, H; Müller M, Böhmer S A, Frank C, Weidner K M, Birchmeier W, Ligensa T, Berndt A, Kosmehl H, Günther B, Müller T, Birchmeier C, Böhmer F D (January 2001). „Negative Regulation of Ros Receptor Tyrosine Kinase Signaling: An Epithelial Function of the Sh2 Domain Protein Tyrosine Phosphatase Shp-1”. J. Cell Biol. (United States) 152 (2): 325–34. DOI:10.1083/jcb.152.2.325. ISSN 0021-9525. PMC 2199605. PMID 11266449. 
  4. ↑ Lechleider, R J; Sugimoto S; Bennett A M; Kashishian A S; Cooper J A; Shoelson S E; Walsh C T; Neel B G (October 1993). „Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyrosine 1009, on the human platelet-derived growth factor receptor”. J. Biol. Chem. (UNITED STATES) 268 (29): 21478–81. ISSN 0021-9258. PMID 7691811. 
  5. ↑ Li, W; Hu P; Skolnik E Y; Ullrich A; Schlessinger J (December 1992). „The SH2 and SH3 domain-containing Nck protein is oncogenic and a common target for phosphorylation by different surface receptors”. Mol. Cell. Biol. (UNITED STATES) 12 (12): 5824–33. DOI:10.1128/MCB.12.12.5824. ISSN 0270-7306. PMC 360522. PMID 1333047. 
  6. ↑ 6,0 6,1 6,2 Braverman, L E; Quilliam L A (February 1999). „Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-containing adapter protein having similar binding and biological properties to Nck”. J. Biol. Chem. (UNITED STATES) 274 (9): 5542–9. DOI:10.1074/jbc.274.9.5542. ISSN 0021-9258. PMID 10026169. 
  7. ↑ Arvidsson, A K; Rupp E; Nånberg E; Downward J; Rönnstrand L; Wennström S; Schlessinger J; Heldin C H i dr.. (October 1994). „Tyr-716 in the platelet-derived growth factor beta-receptor kinase insert is involved in GRB2 binding and Ras activation”. Mol. Cell. Biol. (UNITED STATES) 14 (10): 6715–26. ISSN 0270-7306. PMC 359202. PMID 7935391. 
  8. ↑ Tang, J; Feng G S; Li W (October 1997). „Induced direct binding of the adapter protein Nck to the GTPase-activating protein-associated protein p62 by epidermal growth factor”. Oncogene (ENGLAND) 15 (15): 1823–32. DOI:10.1038/sj.onc.1201351. ISSN 0950-9232. PMID 9362449. 
  9. ↑ Yamamoto, M; Toya Y; Jensen R A; Ishikawa Y (March 1999). „Caveolin is an inhibitor of platelet-derived growth factor receptor signaling”. Exp. Cell Res. (UNITED STATES) 247 (2): 380–8. DOI:10.1006/excr.1998.4379. ISSN 0014-4827. PMID 10066366. 
  10. ↑ Rupp, E; Siegbahn A; Rönnstrand L; Wernstedt C; Claesson-Welsh L; Heldin C H (October 1994). „A unique autophosphorylation site in the platelet-derived growth factor alpha receptor from a heterodimeric receptor complex”. Eur. J. Biochem. (GERMANY) 225 (1): 29–41. DOI:10.1111/j.1432-1033.1994.00029.x. ISSN 0014-2956. PMID 7523122. 
  11. ↑ Seifert, R A; Hart C E; Phillips P E; Forstrom J W; Ross R; Murray M J; Bowen-Pope D F (May 1989). „Two different subunits associate to create isoform-specific platelet-derived growth factor receptors”. J. Biol. Chem. (UNITED STATES) 264 (15): 8771–8. ISSN 0021-9258. PMID 2542288. 
  12. ↑ Maudsley, S; Zamah A M; Rahman N; Blitzer J T; Luttrell L M; Lefkowitz R J; Hall R A (November 2000). „Platelet-Derived Growth Factor Receptor Association with Na+/H+ Exchanger Regulatory Factor Potentiates Receptor Activity”. Mol. Cell. Biol. (UNITED STATES) 20 (22): 8352–63. DOI:10.1128/MCB.20.22.8352-8363.2000. ISSN 0270-7306. PMC 102142. PMID 11046132. 
  13. ↑ Farooqui, T; Kelley T; Coggeshall K M; Rampersaud A A; Yates A J (1999). „GM1 inhibits early signaling events mediated by PDGF receptor in cultured human glioma cells”. Anticancer Res. (GREECE) 19 (6B): 5007–13. ISSN 0250-7005. PMID 10697503. 
  14. ↑ Ekman, Simon; Kallin Anders; Engström Ulla; Heldin Carl-Henrik; Rönnstrand Lars (March 2002). „SHP-2 is involved in heterodimer specific loss of phosphorylation of Tyr771 in the PDGF beta-receptor”. Oncogene (England) 21 (12): 1870–5. DOI:10.1038/sj.onc.1205210. ISSN 0950-9232. PMID 11896619. 
  15. ↑ Matsumoto, T; Yokote K; Take A; Takemoto M; Asaumi S; Hashimoto Y; Matsuda M; Saito Y i dr.. (April 2000). „Differential interaction of CrkII adaptor protein with platelet-derived growth factor alpha- and beta-receptors is determined by its internal tyrosine phosphorylation”. Biochem. Biophys. Res. Commun. (UNITED STATES) 270 (1): 28–33. DOI:10.1006/bbrc.2000.2374. ISSN 0006-291X. PMID 10733900. 
  16. ↑ Yokote, K; Mori S; Hansen K; McGlade J; Pawson T; Heldin C H; Claesson-Welsh L (May 1994). „Direct interaction between Shc and the platelet-derived growth factor beta-receptor”. J. Biol. Chem. (UNITED STATES) 269 (21): 15337–43. ISSN 0021-9258. PMID 8195171. 
  17. ↑ Chen, M; She H; Davis E M; Spicer C M; Kim L; Ren R; Le Beau M M; Li W (September 1998). „Identification of Nck family genes, chromosomal localization, expression, and signaling specificity”. J. Biol. Chem. (UNITED STATES) 273 (39): 25171–8. DOI:10.1074/jbc.273.39.25171. ISSN 0021-9258. PMID 9737977. 
  18. ↑ Chen, M; She H; Kim A; Woodley D T; Li W (November 2000). „Nckβ Adapter Regulates Actin Polymerization in NIH 3T3 Fibroblasts in Response to Platelet-Derived Growth Factor bb”. Mol. Cell. Biol. (UNITED STATES) 20 (21): 7867–80. DOI:10.1128/MCB.20.21.7867-7880.2000. ISSN 0270-7306. PMC 86398. PMID 11027258. 

Literatura

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  • Hart CE, Bowen-Pope DF (1990). „Platelet-derived growth factor receptor: current views of the two-subunit model”. J. Invest. Dermatol. 94 (6 Suppl): 53S–57S. DOI:10.1111/1523-1747.ep12875065. PMID 2161888. 
  • Steer EJ, Cross NC (2002). „Myeloproliferative disorders with translocations of chromosome 5q31-35: role of the platelet-derived growth factor receptor Beta”. Acta Haematol. 107 (2): 113–22. DOI:10.1159/000046641. PMID 11919393. 

Vanjske veze

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Izvor: https://sh.wikipedia.org/w/index.php?title=PDGFRB&oldid=42172757