PDGFRB

PDGFRB
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1GQ5, 1H9O, 1SHA, 2L6W, 2PLD, 2PLE, 3MJG
Identifiers
Aliases	PDGFRB, CD140B, IBGC4, IMF1, JTK12, PDGFR, PDGFR-1, PDGFR1, KOGS, PENTT, platelet derived growth factor receptor beta
External IDs	MGI: 97531 HomoloGene: 1960 GeneCards: PDGFRB
Targeted by Drug
cediranib, crenolanib, linifanib, masitinib, nintedanib, pazopanib, semaxanib, sunitinib, vatalanib[1]
Gene ontology Molecular function • vascular endothelial growth factor binding • kinase activity • platelet-derived growth factor-activated receptor activity • transmembrane receptor protein tyrosine kinase activity • receptor binding • ATP binding • protein kinase activity • platelet-derived growth factor binding • platelet activating factor receptor activity • transferase activity • platelet-derived growth factor receptor binding • protein binding • protein tyrosine kinase activity • protein kinase binding • platelet-derived growth factor beta-receptor activity • nucleotide binding • phosphatidylinositol 3-kinase binding • phosphatidylinositol-4,5-bisphosphate 3-kinase activity • Ras guanyl-nucleotide exchange factor activity • enzyme binding Cellular component • cytoplasm • membrane • focal adhesion • nucleus • apical plasma membrane • lysosome • extracellular exosome • integral component of membrane • plasma membrane • lysosomal lumen • intrinsic component of plasma membrane • cytoplasmic, membrane-bounded vesicle • cytoplasmic vesicle • cell surface Biological process • positive regulation of MAP kinase activity • positive regulation of phospholipase C activity • cell migration involved in vasculogenesis • cardiac myofibril assembly • positive regulation of smooth muscle cell migration • protein phosphorylation • response to lipid • positive regulation of phosphoprotein phosphatase activity • positive regulation of reactive oxygen species metabolic process • metanephric glomerular mesangial cell proliferation involved in metanephros development • positive regulation of ERK1 and ERK2 cascade • cell chemotaxis • inner ear development • metanephric S-shaped body morphogenesis • positive regulation of mitotic nuclear division • platelet-derived growth factor receptor-beta signaling pathway • positive regulation of collagen biosynthetic process • phosphatidylinositol metabolic process • transmembrane receptor protein tyrosine kinase signaling pathway • cell migration involved in coronary angiogenesis • metanephric comma-shaped body morphogenesis • positive regulation of chemotaxis • positive regulation of DNA biosynthetic process • protein autophosphorylation • platelet-derived growth factor receptor signaling pathway • response to toxic substance • positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway • regulation of actin cytoskeleton organization • response to retinoic acid • phosphorylation • response to hyperoxia • retina vasculature development in camera-type eye • metanephric glomerulus morphogenesis • metanephric mesenchymal cell migration • wound healing • cellular response to platelet-derived growth factor stimulus • negative regulation of apoptotic process • response to fluid shear stress • response to estrogen • chemotaxis • metanephric mesenchyme development • response to hydrogen peroxide • phosphatidylinositol-mediated signaling • positive regulation of smooth muscle cell proliferation • response to estradiol • intracellular signal transduction • response to organic cyclic compound • smooth muscle cell chemotaxis • positive regulation of cell migration • aorta morphogenesis • MAPK cascade • positive regulation of phosphatidylinositol 3-kinase activity • metanephric glomerular capillary formation • multicellular organism development • positive regulation of calcium ion import • glycosaminoglycan biosynthetic process • positive regulation of cell proliferation • positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway • positive regulation of phosphatidylinositol 3-kinase signaling • peptidyl-tyrosine phosphorylation • cell migration • signal transduction • positive regulation of GTPase activity • positive regulation of Rho protein signal transduction • G-protein coupled receptor signaling pathway • phosphatidylinositol phosphorylation • positive regulation of hepatic stellate cell activation • positive regulation of fibroblast proliferation • regulation of phosphatidylinositol 3-kinase signaling • positive regulation of apoptotic 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 NM_008809
RefSeq (protein)	NP_002600.1	NP_001139740.1 NP_032835.2
Location (UCSC)	Chr 5: 150.11 – 150.16 Mb	Chr 18: 61.05 – 61.09 Mb
PubMed search	[2]	[3]
Wikidata

View/Edit Human

View/Edit Mouse

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.^[4]

Interactions

PDGFRB has been shown to interact with:

• CRK,^[5]
• Caveolin 1,^[6]
• Grb2,^[7][8][9]
• NCK1,^[7][10]
• NCK2,^[7][11][12]
• PDGFR-α,^[13][14]
• PTPN11,^[15][16]
• RAS p21 protein activator 1,^[17][18]
• SHC1^[19] and
• Sodium-hydrogen antiporter 3 regulator 1.^[20]

See also

• Cluster of differentiation
• Platelet-derived growth factor receptor

References

1. "Drugs that physically interact with Platelet-derived growth factor receptor beta view/edit references on wikidata".
2. "Human PubMed Reference:".
3. "Mouse PubMed Reference:".
4. "Entrez Gene: PDGFRB platelet-derived growth factor receptor, beta polypeptide".
5. 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.
6. 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.
7. 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.
8. 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.
9. 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.
10. 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.
11. 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.
12. 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.
13. 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.
14. 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.
15. 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.
16. 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.
17. 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.
18. 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.
19. 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.
20. 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)