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 3MJG
Identifiers
Symbols	PDGFRB; CD140B; JTK12; PDGF-R-beta; PDGFR; PDGFR1
External IDs	OMIM: 173410 MGI: 97531 HomoloGene: 1960 GeneCards: PDGFRB Gene
Gene Ontology Molecular function • nucleotide binding • receptor activity • platelet activating factor receptor activity • platelet-derived growth factor receptor activity • vascular endothelial growth factor receptor activity • protein binding • ATP binding • transferase activity Cellular component • membrane • integral to membrane Biological process • protein amino acid phosphorylation • signal transduction • transmembrane receptor protein tyrosine kinase signaling pathway • regulation of peptidyl-tyrosine phosphorylation Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	5159	18596
Ensembl	ENSG00000113721	ENSMUSG00000024620
UniProt	P09619	Q003I5
RefSeq (mRNA)	NM_002609	NM_008809
RefSeq (protein)	NP_002600	NP_032835
Location (UCSC)	Chr 5: 149.47 – 149.52 Mb	Chr 18: 61.17 – 61.21 Mb
PubMed search	[1]	[2]

Beta-type platelet-derived growth factor receptor is a protein that in humans is encoded by the PDGFRB 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. 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 5-q 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 PTPN11,^[3][4] NCK1,^[5][6] Grb2,^[7][8][6] Caveolin 1,^[9] PDGFRA,^[10][11] Sodium-hydrogen antiporter 3 regulator 1,^[12] RAS p21 protein activator 1,^[13][14] CRK,^[15] SHC1^[16] and NCK2.^[17][18][6]

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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2895058. ; rendered using PyMOL.
2. ^ "Entrez Gene: PDGFRB platelet-derived growth factor receptor, beta polypeptide". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5159. 
3. ^ Keilhack, H; Müller M, Böhmer S A, Frank C, Weidner K M, Birchmeier W, Ligensa T, Berndt A, Kosmehl H, Günther B, Müller T, Birchmeier C, Böhmer F D (Jan. 2001). "Negative Regulation of Ros Receptor Tyrosine Kinase Signaling: An Epithelial Function of the Sh2 Domain Protein Tyrosine Phosphatase Shp-1". J. Cell Biol. (United States) 152 (2): 325–34. doi:10.1083/jcb.152.2.325. ISSN 0021-9525. PMC 2199605. PMID 11266449. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2199605. 
4. ^ Lechleider, R J; Sugimoto S, Bennett A M, Kashishian A S, Cooper J A, Shoelson S E, Walsh C T, Neel B G (Oct. 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. (UNITED STATES) 268 (29): 21478–81. ISSN 0021-9258. PMID 7691811. 
5. ^ Li, W; Hu P, Skolnik E Y, Ullrich A, Schlessinger J (Dec. 1992). "The SH2 and SH3 domain-containing Nck protein is oncogenic and a common target for phosphorylation by different surface receptors". Mol. Cell. Biol. (UNITED STATES) 12 (12): 5824–33. ISSN 0270-7306. PMC 360522. PMID 1333047. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=360522. 
6. ^ ^{a b c} Braverman, L E; Quilliam L A (Feb. 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. (UNITED STATES) 274 (9): 5542–9. doi:10.1074/jbc.274.9.5542. ISSN 0021-9258. PMID 10026169. 
7. ^ Arvidsson, A K; Rupp E, Nånberg E, Downward J, Rönnstrand L, Wennström S, Schlessinger J, Heldin C H, Claesson-Welsh L (Oct. 1994). "Tyr-716 in the platelet-derived growth factor beta-receptor kinase insert is involved in GRB2 binding and Ras activation". Mol. Cell. Biol. (UNITED STATES) 14 (10): 6715–26. ISSN 0270-7306. PMC 359202. PMID 7935391. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=359202. 
8. ^ Tang, J; Feng G S, Li W (Oct. 1997). "Induced direct binding of the adapter protein Nck to the GTPase-activating protein-associated protein p62 by epidermal growth factor". Oncogene (ENGLAND) 15 (15): 1823–32. doi:10.1038/sj.onc.1201351. ISSN 0950-9232. PMID 9362449. 
9. ^ Yamamoto, M; Toya Y, Jensen R A, Ishikawa Y (Mar. 1999). "Caveolin is an inhibitor of platelet-derived growth factor receptor signaling". Exp. Cell Res. (UNITED STATES) 247 (2): 380–8. doi:10.1006/excr.1998.4379. ISSN 0014-4827. PMID 10066366. 
10. ^ Rupp, E; Siegbahn A, Rönnstrand L, Wernstedt C, Claesson-Welsh L, Heldin C H (Oct. 1994). "A unique autophosphorylation site in the platelet-derived growth factor alpha receptor from a heterodimeric receptor complex". Eur. J. Biochem. (GERMANY) 225 (1): 29–41. doi:10.1111/j.1432-1033.1994.00029.x. ISSN 0014-2956. PMID 7523122. 
11. ^ Seifert, R A; Hart C E, Phillips P E, Forstrom J W, Ross R, Murray M J, Bowen-Pope D F (May. 1989). "Two different subunits associate to create isoform-specific platelet-derived growth factor receptors". J. Biol. Chem. (UNITED STATES) 264 (15): 8771–8. ISSN 0021-9258. PMID 2542288. 
12. ^ Maudsley, S; Zamah A M, Rahman N, Blitzer J T, Luttrell L M, Lefkowitz R J, Hall R A (Nov. 2000). "Platelet-Derived Growth Factor Receptor Association with Na+/H+ Exchanger Regulatory Factor Potentiates Receptor Activity". Mol. Cell. Biol. (UNITED STATES) 20 (22): 8352–63. doi:10.1128/MCB.20.22.8352-8363.2000. ISSN 0270-7306. PMC 102142. PMID 11046132. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=102142. 
13. ^ Farooqui, T; Kelley T, Coggeshall K M, Rampersaud A A, Yates A J (1999). "GM1 inhibits early signaling events mediated by PDGF receptor in cultured human glioma cells". Anticancer Res. (GREECE) 19 (6B): 5007–13. ISSN 0250-7005. PMID 10697503. 
14. ^ Ekman, Simon; Kallin Anders, Engström Ulla, Heldin Carl-Henrik, Rönnstrand Lars (Mar. 2002). "SHP-2 is involved in heterodimer specific loss of phosphorylation of Tyr771 in the PDGF beta-receptor". Oncogene (England) 21 (12): 1870–5. doi:10.1038/sj.onc.1205210. ISSN 0950-9232. PMID 11896619. 
15. ^ Matsumoto, T; Yokote K, Take A, Takemoto M, Asaumi S, Hashimoto Y, Matsuda M, Saito Y, Mori S (Apr. 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. (UNITED STATES) 270 (1): 28–33. doi:10.1006/bbrc.2000.2374. ISSN 0006-291X. PMID 10733900. 
16. ^ Yokote, K; Mori S, Hansen K, McGlade J, Pawson T, Heldin C H, Claesson-Welsh L (May. 1994). "Direct interaction between Shc and the platelet-derived growth factor beta-receptor". J. Biol. Chem. (UNITED STATES) 269 (21): 15337–43. ISSN 0021-9258. PMID 8195171. 
17. ^ Chen, M; She H, Davis E M, Spicer C M, Kim L, Ren R, Le Beau M M, Li W (Sep. 1998). "Identification of Nck family genes, chromosomal localization, expression, and signaling specificity". J. Biol. Chem. (UNITED STATES) 273 (39): 25171–8. doi:10.1074/jbc.273.39.25171. ISSN 0021-9258. PMID 9737977. 
18. ^ Chen, M; She H, Kim A, Woodley D T, Li W (Nov. 2000). "Nckβ Adapter Regulates Actin Polymerization in NIH 3T3 Fibroblasts in Response to Platelet-Derived Growth Factor bb". Mol. Cell. Biol. (UNITED STATES) 20 (21): 7867–80. doi:10.1128/MCB.20.21.7867-7880.2000. ISSN 0270-7306. PMC 86398. PMID 11027258. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=86398. 

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

• MeSH CD140B+Antigen

EPH receptor family

EPHA1 · EPHA2 · EPHA3 · EPHA4 · EPHA5 · EPHA6 · EPHA7 · EPHA8 · EPHB1 · EPHB2 · EPHB3 · EPHB4 · EPHB5 · EPHB6 · EPHX

LTK receptor family

LTK · ALK

TIE receptor family

TIE · TEK

ROR receptor family

ROR1 · ROR2

DDR receptor family

DDR1 · DDR2

PTK7 receptor family

PTK7

RYK receptor family

RYK

MuSK receptor family

MUSK

ROS receptor family

ROS1

AATYK receptor family

AATYK · AATYK2 · AATYK3

AXL receptor family

AXL · MER · TYRO3

RET receptor family

RET

uncatagorised

STYK1

Non-receptor tyrosine kinases (EC 2.7.10.2)
ABL family ABL1 · ARG ACK family ACK1 · TNK1 CSK family CSK · MATK FAK family FAK · PYK2 FES family FES · FER FRK family FRK · BRK · SRMS JAK family JAK1 · JAK2 · JAK3 · TYK2 SRC-A family SRC · FGR · FYN · YES1 SRC-B family BLK · HCK · LCK · LYN TEC family TEC · BMX · BTK · ITK · TXK SYK family SYK · ZAP70

B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6