Go Annotations as Summary Text (Tabular View) (GO Graph)

GO curators for mouse genes have assigned the following annotations to the gene product of Pdgfrb. (This text reflects annotations as of Tuesday, May 21, 2013.)

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Summary from NCBI RefSeq

[Summary is not available for the mouse gene. This summary is for the human ortholog.] 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. [provided by RefSeq, Jul 2008]

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Summary text based on GO annotations supported by experimental evidence in mouse

• Researchers have inferred from direct assay, that the gene product of Pdgfrb
  • participates in the following biological processes:
    • peptidyl-tyrosine phosphorylation ^[12]
    • positive regulation of chemotaxis ^[6]
    • positive regulation of ERK1 and ERK2 cascade ^[13]
    • positive regulation of MAP kinase activity ^[13]
    • positive regulation of mitosis ^[13]
    • positive regulation of phosphatidylinositol 3-kinase cascade ^[13]
    • protein autophosphorylation ^[12]
    • signal transduction ^[8]
  • performs the following molecular functions:
    • signal transducer activity ^[8]
  • is located in the following cellular components:
    • cytoplasm ^[1]
• The gene product of Pdgfrb has been shown to bind to the gene products of Pdgfrb, Pik3r1, Sh2b1, Slc9a3r2. ^{[7, 11]} Researchers have inferred, based on physical interactions, that the gene product of Pdgfrb
  • performs the following molecular functions:
    • receptor binding ^[11]
• Researchers have inferred, based on phenotypic analysis of mouse mutants, that the gene product of Pdgfrb
  • participates in the following biological processes:
    • cell migration involved in coronary angiogenesis ^[12]
    • cell migration involved in vasculogenesis ^[12]
    • in utero embryonic development ^[10]
    • kidney development ^[10]
    • metanephric glomerular mesangial cell proliferation involved in metanephros development ^[5]
    • nitrogen compound metabolic process ^[10]
    • platelet-derived growth factor receptor signaling pathway ^[10]
    • positive regulation of calcium ion import ^[6]
    • positive regulation of DNA biosynthetic process ^[6]
    • positive regulation of ERK1 and ERK2 cascade ^[12]
    • positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway ^[6]
    • positive regulation of reactive oxygen species metabolic process ^[6]
    • positive regulation of smooth muscle cell migration ^[2]
    • positive regulation of smooth muscle cell proliferation ^[2]
    • regulation of peptidyl-tyrosine phosphorylation ^[8]
    • retina vasculature development in camera-type eye ^[12]
    • skeletal system morphogenesis ^[10]
    • smooth muscle tissue development ^[10]
    • tissue homeostasis ^[10]
  • performs the following molecular functions:
    • kinase activity ^[3]
• Researchers have inferred, based on genetic interactions, that the gene product of Pdgfrb
  • participates in the following biological processes:
    • adrenal gland development based on interactions with Pdgfra ^[9]
    • aorta morphogenesis based on interactions with Lrp1 ^[14]
    • cardiac myofibril assembly based on interactions with Pdgfra ^[4]
    • metanephric glomerular capillary formation based on interactions with Pdgfra ^[4]
    • positive regulation of smooth muscle cell migration based on interactions with Lrp1 ^[14]
    • regulation of actin cytoskeleton organization based on interactions with Lrp1 ^[14]
    • retina vasculature development in camera-type eye based on interactions with Pdgfra ^[4]
    • smooth muscle cell chemotaxis based on interactions with Lrp1 ^[14]

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Summary text based on GO annotations supported by experimental evidence in other organisms

• From comparative sequence analysis (see table for details), MGI curators have determined that the gene product of Pdgfrb:
  • participates in the following biological processes:
    • cell chemotaxis
    • cell migration
    • cellular response to platelet-derived growth factor stimulus
    • glycosaminoglycan biosynthetic process
    • intracellular protein kinase cascade
    • metanephric mesenchymal cell migration
    • negative regulation of apoptotic process
    • peptidyl-tyrosine phosphorylation
    • phosphatidylinositol metabolic process
    • phosphatidylinositol-mediated signaling
    • platelet-derived growth factor receptor signaling pathway
    • platelet-derived growth factor receptor-beta signaling pathway
    • positive regulation of cell migration
    • positive regulation of cell proliferation
    • positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway
    • positive regulation of collagen biosynthetic process
    • positive regulation of ERK1 and ERK2 cascade
    • positive regulation of phosphatidylinositol 3-kinase activity
    • positive regulation of phospholipase C activity
    • positive regulation of phosphoprotein phosphatase activity
    • positive regulation of smooth muscle cell migration
    • positive regulation of smooth muscle cell proliferation
    • protein autophosphorylation
    • signal transduction
    • transforming growth factor beta receptor signaling pathway
  • performs the following molecular functions:
    • phosphatidylinositol 3-kinase binding
    • platelet-derived growth factor beta-receptor activity
    • platelet-derived growth factor binding
    • platelet-derived growth factor receptor binding
    • platelet-derived growth factor-activated receptor activity
    • protein tyrosine kinase activity
    • receptor binding
    • vascular endothelial growth factor binding
  • is located in the following cellular components:
    • apical plasma membrane
    • cytoplasm
    • intrinsic to plasma membrane
    • membrane
    • nucleus
    • plasma membrane

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Summary text based on GO annotations supported by structural data

• Pdgfrb encodes a protein or proteins that contain the following InterPro domains: Immunoglobulin, Immunoglobulin subtype, Immunoglobulin subtype 2, Immunoglobulin-like domain, Immunoglobulin-like fold, Platelet-derived growth factor receptor beta, Protein kinase, ATP binding site, Protein kinase, catalytic domain, Protein kinase-like domain, Serine-threonine/tyrosine-protein kinase catalytic domain, Tyrosine-protein kinase, active site, Tyrosine-protein kinase, catalytic domain, Tyrosine-protein kinase, CSF-1/PDGF receptor, Tyrosine-protein kinase, receptor class III, conserved site, Tyrosine-protein kinase, vascular endothelial growth factor receptor (VEGFR), N-terminal, indicating that the gene product:
  • participates in the following biological processes:
    • protein phosphorylation
    • transmembrane receptor protein tyrosine kinase signaling pathway
    • vascular endothelial growth factor receptor signaling pathway
  • performs the following molecular functions:
    • ATP binding
    • protein kinase activity
    • transferase activity, transferring phosphorus-containing groups
    • transmembrane receptor protein tyrosine kinase activity
    • vascular endothelial growth factor-activated receptor activity
  • is located in the following cellular components:
    • integral to membrane
    • integral to plasma membrane

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Summary text for additional MGI annotations

• Automated translation to GO terms of SwissProt keywords that describe Pdgfrb indicates that it:
  • participates in the following biological processes:
    • chemotaxis
    • multicellular organismal development
    • phosphorylation
  • performs the following molecular functions:
    • ATP binding
    • nucleotide binding
    • transferase activity
  • is located in the following cellular components:
    • cytoplasmic vesicle
    • integral to membrane
    • lysosome
• Pdgfrb has been associated with the Enzyme Commission numbers: 2.7.10.1, which implies that the gene product:
  • performs the following molecular functions:
    • transmembrane receptor protein tyrosine kinase activity

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References

1. Fukumoto Y et al. (2011) Role of scaffold protein afadin dilute domain-interacting protein (ADIP) in platelet-derived growth factor-induced cell movement by activating Rac protein through Vav2 protein. J Biol Chem, 286:43537-48. (PubMed:22027834)
2. Hellstrom M et al. (1999) Role of PDGF-B and PDGFR-beta in recruitment of vascular smooth muscle cells and pericytes during embryonic blood vessel formation in the mouse. Development, 126:3047-55. (PubMed:10375497)
3. Holgado-Madruga M et al. (2003) Gab1 is an integrator of cell death versus cell survival signals in oxidative stress. Mol Cell Biol, 23:4471-84. (PubMed:12808090)
4. Klinghoffer RA et al. (2001) The two PDGF receptors maintain conserved signaling in vivo despite divergent embryological functions. Mol Cell, 7:343-54. (PubMed:11239463)
5. Lindahl P et al. (1998) Paracrine PDGF-B/PDGF-Rbeta signaling controls mesangial cell development in kidney glomeruli. Development, 125:3313-22. (PubMed:9693135)
6. Ricono JM et al. (2009) PDGF receptor-{beta} modulates metanephric mesenchyme chemotaxis induced by PDGF AA. Am J Physiol Renal Physiol, 296:F406-17. (PubMed:19019919)
7. Riedel H et al. (2000) PSM, a mediator of PDGF-BB-, IGF-I-, and insulin-stimulated mitogenesis. Oncogene, 19:39-50. (PubMed:10644978)
8. Saito Y et al. (2002) Protein kinase C-alpha and protein kinase C-epsilon are required for Grb2-associated binder-1 tyrosine phosphorylation in response to platelet-derived growth factor. J Biol Chem, 277:23216-22. (PubMed:11940581)
9. Schmahl J et al. (2008) The PDGF signaling pathway controls multiple steroid-producing lineages. Genes Dev, 22:3255-67. (PubMed:19056881)
10. Schmahl J et al. (2007) PDGF signaling specificity is mediated through multiple immediate early genes. Nat Genet, 39:52-60. (PubMed:17143286)
11. Takahashi Y et al. (2006) PTEN tumor suppressor associates with NHERF proteins to attenuate PDGF receptor signaling. EMBO J, 25:910-20. (PubMed:16456542)
12. Tallquist MD et al. (2003) Additive Effects of PDGF Receptor beta Signaling Pathways in Vascular Smooth Muscle Cell Development. PLoS Biol, 1:288-99. (PubMed:14624252)
13. Wagner B et al. (2007) Mitogenic signaling via platelet-derived growth factor beta in metanephric mesenchymal cells. J Am Soc Nephrol, 18:2903-11. (PubMed:17942966)
14. Zhou L et al. (2009) LRP1 regulates architecture of the vascular wall by controlling PDGFRbeta-dependent phosphatidylinositol 3-kinase activation. PLoS One, 4:e6922. (PubMed:19742316)

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Gene Ontology Evidence Code Abbreviations:

EXP Inferred from experiment

IC Inferred by curator

IDA Inferred from direct assay

IEA Inferred from electronic annotation

IGI Inferred from genetic interaction

IMP Inferred from mutant phenotype

IPI Inferred from physical interaction

ISS Inferred from sequence or structural similarity

ISO Inferred from sequence orthology

ISA Inferred from sequence alignment

ISM Inferred from sequence model

NAS Non-traceable author statement

ND No biological data available

RCA Reviewed computational analysis

TAS Traceable author statement

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