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Title: Pdgfrb  
Author: World Heritage Encyclopedia
Language: English
Subject: Kinase insert domain receptor, LRP1, DDR1, TEK tyrosine kinase, Anaplastic lymphoma kinase
Publisher: World Heritage Encyclopedia


Platelet-derived growth factor receptor, beta polypeptide

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
Symbols  ; CD140B; IBGC4; IMF1; JTK12; PDGFR; PDGFR-1; PDGFR1
External IDs ChEMBL: GeneCards:
EC number
RNA expression pattern
Species Human Mouse
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
PubMed search

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


PDGFRB has been shown to interact with PTPN11,[3][4] NCK1,[5][6] Grb2,[6][7][8] Caveolin 1,[9] PDGFRA,[10][11] Sodium-hydrogen antiporter 3 regulator 1,[12] RAS p21 protein activator 1,[13][14] CRK,[15] SHC1[16] and NCK2.[6][17][18]

See also


  1. ^  ; 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.  
  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.  
  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.  
  6. ^ a b c 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.  
  7. ^ Arvidsson, A K; Rupp E; Nånberg E; Downward J; Rönnstrand L; Wennström S; Schlessinger J; Heldin C H; Claesson-Welsh L (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.  
  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.  
  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.  
  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.  
  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.  
  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.  
  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.  
  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.  
  15. ^ Matsumoto, T; Yokote K; Take A; Takemoto M; Asaumi S; Hashimoto Y; Matsuda M; Saito Y; Mori S (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.  
  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.  
  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.  
  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.  

Further reading

External links

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