PDGFRA

Platelet-derived growth factor receptor, alpha polypeptide
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1GQ5​
Identifiers
Symbols	PDGFRA ; CD140A; PDGFR-2; PDGFR2; RHEPDGFRA
External IDs	OMIM: 173490 MGI: 97530 HomoloGene: 31361 ChEMBL: 2007 GeneCards: PDGFRA Gene
EC number	2.7.10.1
Gene ontology Molecular function • protein kinase activity • transmembrane receptor protein tyrosine kinase activity • platelet-derived growth factor alpha-receptor activity • vascular endothelial growth factor-activated receptor activity • platelet-derived growth factor receptor binding • protein binding • ATP binding • protein complex binding • vascular endothelial growth factor binding • protein homodimerization activity • phosphatidylinositol 3-kinase binding • platelet-derived growth factor binding Cellular component • nucleus • cytoplasm • cytosol • plasma membrane • integral component of plasma membrane • microvillus • external side of plasma membrane • membrane • intrinsic component of plasma membrane • protein complex Biological process • luteinization • in utero embryonic development • cell activation • hematopoietic progenitor cell differentiation • epidermal growth factor receptor signaling pathway • positive regulation of cytosolic calcium ion concentration • estrogen metabolic process • positive regulation of cell proliferation • fibroblast growth factor receptor signaling pathway • response to inorganic substance • negative regulation of platelet activation • positive regulation of phospholipase C activity • positive regulation of phosphatidylinositol 3-kinase signaling • viral process • peptidyl-tyrosine phosphorylation • signal transduction involved in regulation of gene expression • extracellular matrix organization • lung development • adrenal gland development • positive regulation of cell migration • male genitalia development • response to estradiol • Leydig cell differentiation • response to cytokine • cellular response to reactive oxygen species • platelet-derived growth factor receptor-alpha signaling pathway • positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway • Fc-epsilon receptor signaling pathway • wound healing • gliogenesis • odontogenesis of dentin-containing tooth • positive regulation of phosphatidylinositol 3-kinase activity • innate immune response • positive regulation of DNA replication • protein autophosphorylation • platelet-derived growth factor receptor signaling pathway • neurotrophin TRK receptor signaling pathway • phosphatidylinositol-mediated signaling • positive regulation of fibroblast proliferation • embryonic digestive tract morphogenesis • embryonic cranial skeleton morphogenesis • embryonic skeletal system morphogenesis • inner ear development • regulation of chemotaxis • cardiac myofibril assembly • response to hyperoxia • palate development • face morphogenesis • cell chemotaxis • retina vasculature development in camera-type eye • positive regulation of ERK1 and ERK2 cascade • platelet aggregation • cellular response to amino acid stimulus • metanephric glomerular capillary formation • regulation of actin cytoskeleton reorganization • regulation of mesenchymal stem cell differentiation Sources: Amigo / QuickGO
RNA expression pattern
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: 54.23 – 54.3 Mb	Chr 5: 75.15 – 75.2 Mb
PubMed search

Platelet-derived growth factor receptor, alpha polypeptide is a protein that in humans is encoded by the PDGFRA gene.

Function

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

PDGFRA has been shown to interact with:

• CRK,^[2][3]
• Caveolin 1,^[4]
• Cbl gene,^[5]
• PDGFC,^[6]
• PDGFR-β,^[7][8]
• PLCG1,^[9] and
• Sodium-hydrogen antiporter 3 regulator 1.^[10]

See also

• Platelet-derived growth factor receptor

References

1. "Entrez Gene: PDGFRA platelet-derived growth factor receptor, alpha polypeptide".
2. Yokote K, Hellman U, Ekman S, Saito Y, Rönnstrand L, Saito Y, Heldin CH, Mori S (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, 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. 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. doi:10.1128/mcb.17.8.4597. PMC 232313. PMID 9234717.
6. Gilbertson DG, Duff ME, West JW, Kelly JD, Sheppard PO, Hofstrand PD, Gao Z, Shoemaker K, Bukowski TR, Moore M, Feldhaus AL, Humes JM, Palmer TE, Hart CE (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. doi:10.1111/j.1432-1033.1994.00029.x. PMID 7523122.
8. Seifert RA, Hart CE, Phillips PE, Forstrom JW, Ross R, Murray MJ, Bowen-Pope DF (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, Carpenter G, Heldin CH, Claesson-Welsh L (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. doi:10.1074/jbc.270.13.7773. PMID 7535778.
10. Maudsley S, Zamah AM, Rahman N, Blitzer JT, Luttrell LM, Lefkowitz RJ, Hall RA (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

• 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, Shiraga S, Bainbridge T, Morich J, Heinrich MC (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.