Open Access Articles- Top Results for PDGFRA


External IDsOMIM173490 MGI97530 HomoloGene31361 IUPHAR: 1803 ChEMBL: 2007 GeneCards: PDGFRA Gene
EC number2.7.10.1
RNA expression pattern
File:PBB GE PDGFRA 203131 at tn.png
More reference expression data
RefSeq (mRNA)NM_006206NM_001083316
RefSeq (protein)NP_006197NP_001076785
Location (UCSC)Chr 4:
55.1 – 55.16 Mb
Chr 5:
75.15 – 75.2 Mb
PubMed search[1][2]

Alpha-type platelet-derived growth factor receptor is a protein that in humans is encoded by the PDGFRA 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. Studies in knockout mice, where homozygosity is lethal, indicate that the alpha form of the platelet-derived growth factor receptor is particularly important for kidney development since mice heterozygous for the receptor exhibit defective kidney phenotypes.[1]


PDGFRA has been shown to interact with:

See also


  1. ^ "Entrez Gene: PDGFRA platelet-derived growth factor receptor, alpha polypeptide". 
  2. ^ Yokote K, Hellman U, Ekman S, Saito Y, Rönnstrand L, Saito Y et al. (March 1998). "Identification of Tyr-762 in the platelet-derived growth factor alpha-receptor as the binding site for Crk proteins". Oncogene 16 (10): 1229–39. PMID 9546424. doi:10.1038/sj.onc.1201641. 
  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. PMID 10733900. doi:10.1006/bbrc.2000.2374. 
  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. PMID 10066366. doi:10.1006/excr.1998.4379. 
  5. ^ Bonita DP, Miyake S, Lupher ML, Langdon WY, Band H (August 1997). "Phosphotyrosine binding domain-dependent upregulation of the platelet-derived growth factor receptor alpha signaling cascade by transforming mutants of Cbl: implications for Cbl's function and oncogenicity". Mol. Cell. Biol. 17 (8): 4597–610. PMC 232313. PMID 9234717. 
  6. ^ Gilbertson DG, Duff ME, West JW, Kelly JD, Sheppard PO, Hofstrand PD et al. (July 2001). "Platelet-derived growth factor C (PDGF-C), a novel growth factor that binds to PDGF alpha and beta receptor". J. Biol. Chem. 276 (29): 27406–14. PMID 11297552. doi:10.1074/jbc.M101056200. 
  7. ^ 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. PMID 7523122. doi:10.1111/j.1432-1033.1994.00029.x. 
  8. ^ 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. 
  9. ^ Eriksson A, Nånberg E, Rönnstrand L, Engström U, Hellman U, Rupp E et al. (March 1995). "Demonstration of functionally different interactions between phospholipase C-gamma and the two types of platelet-derived growth factor receptors". J. Biol. Chem. 270 (13): 7773–81. PMID 7535778. doi:10.1074/jbc.270.13.7773. 
  10. ^ 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. PMC 102142. PMID 11046132. doi:10.1128/mcb.20.22.8352-8363.2000. 

Further reading

  • 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. PMID 2161888. doi:10.1111/1523-1747.ep12875065. 
  • Corless CL, Schroeder A, Griffith D, Town A, McGreevey L, Harrell P et al. (2005). "PDGFRA mutations in gastrointestinal stromal tumors: frequency, spectrum and in vitro sensitivity to imatinib". J. Clin. Oncol. 23 (23): 5357–64. PMID 15928335. doi:10.1200/JCO.2005.14.068. 
  • Lasota J, Miettinen M (2007). "KIT and PDGFRA mutations in gastrointestinal stromal tumors (GISTs)". Semin Diagn Pathol 23 (2): 91–102. PMID 17193822. doi:10.1053/j.semdp.2006.08.006. 

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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