PDGFRB

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Platelet-derived growth factor receptor, beta polypeptide
PDGFR-beta 3MJG.png
Ribbon image of two molecules of human PDGF receptor beta (yellow and magenta) in complex with dimeric PDGF-B (cyan and green).[1]
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols PDGFRB ; CD140B; IBGC4; IMF1; JTK12; PDGFR; PDGFR-1; PDGFR1
External IDs OMIM173410 MGI97531 HomoloGene1960 ChEMBL: 1913 GeneCards: PDGFRB Gene
EC number 2.7.10.1
RNA expression pattern
PBB GE PDGFRB 202273 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 5159 18596
Ensembl ENSG00000113721 ENSMUSG00000024620
UniProt P09619 P05622
RefSeq (mRNA) NM_002609 NM_001146268
RefSeq (protein) NP_002600 NP_001139740
Location (UCSC) Chr 5:
149.49 – 149.54 Mb
Chr 18:
61.05 – 61.09 Mb
PubMed search [1] [2]

Beta-type platelet-derived growth factor receptor is a protein that in humans is encoded by the PDGFRB gene.

Function[edit]

This gene encodes a cell surface tyrosine kinase receptor for members of the platelet-derived growth factor family. These growth factors are mitogens for cells of mesenchymal origin. The identity of the growth factor bound to a receptor monomer determines whether the functional receptor is a homodimer or a heterodimer, composed of both platelet-derived growth factor receptor alpha and beta polypeptides. This gene is flanked on chromosome 5 by the genes for granulocyte-macrophage colony-stimulating factor and macrophage-colony stimulating factor receptor; all three genes may be implicated in the 5q- syndrome. A translocation between chromosomes 5 and 12, that fuses this gene to that of the translocation, ETV6, leukemia gene, results in chronic myeloproliferative disorder with eosinophilia.[2]

Interactions[edit]

PDGFRB has been shown to interact with:

See also[edit]

References[edit]

  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. ^ Matsumoto T, Yokote K, Take A, Takemoto M, Asaumi S, Hashimoto Y et al. (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. 270 (1): 28–33. doi:10.1006/bbrc.2000.2374. PMID 10733900. 
  4. ^ Yamamoto M, Toya Y, Jensen RA, Ishikawa Y (March 1999). "Caveolin is an inhibitor of platelet-derived growth factor receptor signaling". Exp. Cell Res. 247 (2): 380–8. doi:10.1006/excr.1998.4379. PMID 10066366. 
  5. ^ a b c Braverman LE, Quilliam LA (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. 274 (9): 5542–9. doi:10.1074/jbc.274.9.5542. PMID 10026169. 
  6. ^ Arvidsson AK, Rupp E, Nånberg E, Downward J, Rönnstrand L, Wennström S et al. (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. 14 (10): 6715–26. PMC 359202. PMID 7935391.  Vancouver style error (help)
  7. ^ Tang J, Feng GS, 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 15 (15): 1823–32. doi:10.1038/sj.onc.1201351. PMID 9362449. 
  8. ^ Li W, Hu P, Skolnik EY, 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. 12 (12): 5824–33. doi:10.1128/MCB.12.12.5824. PMC 360522. PMID 1333047. 
  9. ^ Chen M, She H, Davis EM, Spicer CM, Kim L, Ren R et al. (September 1998). "Identification of Nck family genes, chromosomal localization, expression, and signaling specificity". J. Biol. Chem. 273 (39): 25171–8. doi:10.1074/jbc.273.39.25171. PMID 9737977. 
  10. ^ Chen M, She H, Kim A, Woodley DT, Li W (November 2000). "Nckbeta adapter regulates actin polymerization in NIH 3T3 fibroblasts in response to platelet-derived growth factor bb". Mol. Cell. Biol. 20 (21): 7867–80. doi:10.1128/mcb.20.21.7867-7880.2000. PMC 86398. PMID 11027258. 
  11. ^ Rupp E, Siegbahn A, Rönnstrand L, Wernstedt C, Claesson-Welsh L, Heldin CH (October 1994). "A unique autophosphorylation site in the platelet-derived growth factor alpha receptor from a heterodimeric receptor complex". Eur. J. Biochem. 225 (1): 29–41. doi:10.1111/j.1432-1033.1994.00029.x. PMID 7523122.  Vancouver style error (help)
  12. ^ Seifert RA, Hart CE, Phillips PE, Forstrom JW, Ross R, Murray MJ et al. (May 1989). "Two different subunits associate to create isoform-specific platelet-derived growth factor receptors". J. Biol. Chem. 264 (15): 8771–8. PMID 2542288. 
  13. ^ Keilhack H, Müller M, Böhmer SA, Frank C, Weidner KM, Birchmeier W et al. (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. 152 (2): 325–34. doi:10.1083/jcb.152.2.325. PMC 2199605. PMID 11266449.  Vancouver style error (help)
  14. ^ Lechleider RJ, Sugimoto S, Bennett AM, Kashishian AS, Cooper JA, Shoelson SE et al. (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. 268 (29): 21478–81. PMID 7691811. 
  15. ^ Farooqui T, Kelley T, Coggeshall KM, Rampersaud AA, Yates AJ. "GM1 inhibits early signaling events mediated by PDGF receptor in cultured human glioma cells". Anticancer Res. 19 (6B): 5007–13. PMID 10697503. 
  16. ^ Ekman S, Kallin A, Engström U, Heldin CH, Rönnstrand L (March 2002). "SHP-2 is involved in heterodimer specific loss of phosphorylation of Tyr771 in the PDGF beta-receptor". Oncogene 21 (12): 1870–5. doi:10.1038/sj.onc.1205210. PMID 11896619.  Vancouver style error (help)
  17. ^ Yokote K, Mori S, Hansen K, McGlade J, Pawson T, Heldin CH et al. (May 1994). "Direct interaction between Shc and the platelet-derived growth factor beta-receptor". J. Biol. Chem. 269 (21): 15337–43. PMID 8195171. 
  18. ^ Maudsley S, Zamah AM, Rahman N, Blitzer JT, Luttrell LM, Lefkowitz RJ et al. (November 2000). "Platelet-derived growth factor receptor association with Na(+)/H(+) exchanger regulatory factor potentiates receptor activity". Mol. Cell. Biol. 20 (22): 8352–63. doi:10.1128/mcb.20.22.8352-8363.2000. PMC 102142. PMID 11046132. 

Further reading[edit]

  • 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. 

External links[edit]