PDGFRA

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Platelet-derived growth factor receptor, alpha polypeptide
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols PDGFRA ; CD140A; PDGFR-2; PDGFR2; RHEPDGFRA
External IDs OMIM173490 MGI97530 HomoloGene31361 ChEMBL: 2007 GeneCards: PDGFRA Gene
EC number 2.7.10.1
RNA expression pattern
PBB GE PDGFRA 203131 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 5156 18595
Ensembl ENSG00000134853 ENSMUSG00000029231
UniProt P16234 P26618
RefSeq (mRNA) NM_006206 NM_001083316
RefSeq (protein) NP_006197 NP_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.

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. 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]

Interactions[edit]

PDGFRA has been shown to interact with:

See also[edit]

References[edit]

  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. doi:10.1038/sj.onc.1201641. PMID 9546424. 
  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. ^ 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. doi:10.1074/jbc.M101056200. PMID 11297552. 
  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. 
  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. 
  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. 

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. 
  • 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. doi:10.1200/JCO.2005.14.068. PMID 15928335. 
  • Lasota J, Miettinen M (2007). "KIT and PDGFRA mutations in gastrointestinal stromal tumors (GISTs)". Semin Diagn Pathol 23 (2): 91–102. doi:10.1053/j.semdp.2006.08.006. PMID 17193822. 

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