PDGFRB

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 List of PDB id codes 1GQ5​, 1H9O​, 1LWP​, 1SHA​, 2L6W​, 2PLD​, 2PLE​, 3MJG​
Identifiers
Symbols	PDGFRB ; CD140B; IBGC4; IMF1; JTK12; PDGFR; PDGFR-1; PDGFR1
External IDs	OMIM: 173410 MGI: 97531 HomoloGene: 1960 ChEMBL: 1913 GeneCards: PDGFRB Gene
EC number	2.7.10.1
Gene ontology Molecular function • protein tyrosine kinase activity • platelet activating factor receptor activity • platelet-derived growth factor-activated receptor activity • platelet-derived growth factor beta-receptor activity • receptor binding • platelet-derived growth factor receptor binding • protein binding • ATP binding • protein kinase binding • vascular endothelial growth factor binding • phosphatidylinositol 3-kinase binding • platelet-derived growth factor binding Cellular component • nucleus • cytoplasm • plasma membrane • focal adhesion • cell surface • membrane • integral component of membrane • cytoplasmic membrane-bounded vesicle • apical plasma membrane • intrinsic component of plasma membrane • lysosomal lumen • extracellular exosome Biological process • in utero embryonic development • tissue homeostasis • glycosaminoglycan biosynthetic process • signal transduction • epidermal growth factor receptor signaling pathway • G-protein coupled receptor signaling pathway • positive regulation of cell proliferation • fibroblast growth factor receptor signaling pathway • response to toxic substance • positive regulation of phospholipase C activity • positive regulation of phosphatidylinositol 3-kinase signaling • positive regulation of smooth muscle cell migration • cell migration • peptidyl-tyrosine phosphorylation • adrenal gland development • positive regulation of cell migration • response to estradiol • positive regulation of phosphoprotein phosphatase activity • response to retinoic acid • regulation of actin cytoskeleton organization • positive regulation of collagen biosynthetic process • response to fluid shear stress • cell migration involved in vasculogenesis • metanephric mesenchymal cell migration • platelet-derived growth factor receptor-beta signaling pathway • positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway • aorta morphogenesis • cellular response to platelet-derived growth factor stimulus • positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway • Fc-epsilon receptor signaling pathway • wound healing • response to hydrogen peroxide • negative regulation of apoptotic process • positive regulation of MAP kinase activity • positive regulation of phosphatidylinositol 3-kinase activity • innate immune response • positive regulation of mitotic nuclear division • phosphatidylinositol metabolic process • protein autophosphorylation • platelet-derived growth factor receptor signaling pathway • neurotrophin TRK receptor signaling pathway • phosphatidylinositol-mediated signaling • positive regulation of smooth muscle cell proliferation • skeletal system morphogenesis • smooth muscle tissue development • inner ear development • regulation of peptidyl-tyrosine phosphorylation • positive regulation of chemotaxis • cardiac myofibril assembly • response to hyperoxia • cell chemotaxis • cell migration involved in coronary angiogenesis • retina vasculature development in camera-type eye • positive regulation of ERK1 and ERK2 cascade • smooth muscle cell chemotaxis • metanephric mesenchyme development • metanephric glomerular mesangial cell proliferation involved in metanephros development • metanephric glomerular capillary formation • metanephric comma-shaped body morphogenesis • metanephric S-shaped body morphogenesis • positive regulation of calcium ion import • positive regulation of reactive oxygen species metabolic process • positive regulation of DNA biosynthetic process Sources: Amigo / QuickGO
RNA expression pattern
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: 150.11 – 150.16 Mb	Chr 18: 61.05 – 61.09 Mb
PubMed search

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

PDGFRB has been shown to interact with:

• CRK,^[3]
• Caveolin 1,^[4]
• Grb2,^[5][6][7]
• NCK1,^[5][8]
• NCK2,^[5][9][10]
• PDGFR-α,^[11][12]
• PTPN11,^[13][14]
• RAS p21 protein activator 1,^[15][16]
• SHC1^[17] and
• Sodium-hydrogen antiporter 3 regulator 1.^[18]

See also

• Cluster of differentiation
• Platelet-derived growth factor receptor

References

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, 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. 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, Schlessinger J, Heldin CH, 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. 14 (10): 6715–26. doi:10.1128/mcb.14.10.6715. PMC 359202. PMID 7935391.
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, Le Beau MM, Li W (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.
12. 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.
13. Keilhack H, Müller M, Böhmer SA, Frank C, Weidner KM, Birchmeier W, Ligensa T, Berndt A, Kosmehl H, Günther B, Müller T, Birchmeier C, Böhmer FD (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.
14. Lechleider RJ, Sugimoto S, Bennett AM, Kashishian AS, Cooper JA, Shoelson SE, Walsh CT, Neel BG (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 (1999). "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.
17. Yokote K, Mori S, Hansen K, McGlade J, Pawson T, Heldin CH, Claesson-Welsh L (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, 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.
• 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

• CD140B Antigen at the US National Library of Medicine Medical Subject Headings (MeSH)