FRS2

From Wikipedia, the free encyclopedia

Fibroblast growth factor receptor substrate 2

PDB rendering based on 1xr0.

Available structures: 1xr0

Identifiers

Symbol(s)

FRS2; SNT1; FRS2A; FRS2alpha; SNT; SNT-1

External IDs

OMIM: 607743 MGI: 1100860 HomoloGene: 4846

Gene ontology
Molecular Function:	• transmembrane receptor protein tyrosine kinase adaptor protein activity • transmembrane receptor protein tyrosine kinase docking protein activity • insulin receptor binding • protein binding • regulator of G-protein signaling activity • phosphatase activator activity
Cellular Component:	• membrane fraction • cytoplasm • plasma membrane • integral to plasma membrane
Biological Process:	• activation of MAPK activity • induction of an organ • transmembrane receptor protein tyrosine phosphatase signaling pathway • G-protein coupled receptor protein signaling pathway • fibroblast growth factor receptor signaling pathway • determination of anterior/posterior axis, embryo • gastrulation (sensu Mammalia) • forebrain development • neuroblast proliferation (sensu Vertebrata) • optic placode formation involved in camera-type eye

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001042555 (mRNA)
NP_001036020 (protein)

XM_984180 (mRNA)
XP_989274 (protein)

Location

Chr 12: 68.15 - 68.26 Mb

Chr 10: 116.47 - 116.55 Mb

Pubmed search

[1]

[2]

Fibroblast growth factor receptor substrate 2, also known as FRS2, is a human gene.^[1]

[edit] References

^ Entrez Gene: FRS2 Fibroblast growth factor receptor substrate 2.

[edit] Further reading

Wang JK, Xu H, Li HC, Goldfarb M (1996). "Broadly expressed SNT-like proteins link FGF receptor stimulation to activators of Ras.". Oncogene 13 (4): 721-9. PMID 8761293.
Ong SH, Goh KC, Lim YP, et al. (1996). "Suc1-associated neurotrophic factor target (SNT) protein is a major FGF-stimulated tyrosine phosphorylated 90-kDa protein which binds to the SH2 domain of GRB2.". Biochem. Biophys. Res. Commun. 225 (3): 1021-6. doi:10.1006/bbrc.1996.1288. PMID 8780727.
Kouhara H, Hadari YR, Spivak-Kroizman T, et al. (1997). "A lipid-anchored Grb2-binding protein that links FGF-receptor activation to the Ras/MAPK signaling pathway.". Cell 89 (5): 693-702. PMID 9182757.
Hadari YR, Kouhara H, Lax I, Schlessinger J (1998). "Binding of Shp2 tyrosine phosphatase to FRS2 is essential for fibroblast growth factor-induced PC12 cell differentiation.". Mol. Cell. Biol. 18 (7): 3966-73. PMID 9632781.
Xu H, Lee KW, Goldfarb M (1998). "Novel recognition motif on fibroblast growth factor receptor mediates direct association and activation of SNT adapter proteins.". J. Biol. Chem. 273 (29): 17987-90. PMID 9660748.
Meakin SO, MacDonald JI, Gryz EA, et al. (1999). "The signaling adapter FRS-2 competes with Shc for binding to the nerve growth factor receptor TrkA. A model for discriminating proliferation and differentiation.". J. Biol. Chem. 274 (14): 9861-70. PMID 10092678.
Lim YP, Low BC, Lim J, et al. (1999). "Association of atypical protein kinase C isotypes with the docker protein FRS2 in fibroblast growth factor signaling.". J. Biol. Chem. 274 (27): 19025-34. PMID 10383403.
Ong SH, Guy GR, Hadari YR, et al. (2000). "FRS2 proteins recruit intracellular signaling pathways by binding to diverse targets on fibroblast growth factor and nerve growth factor receptors.". Mol. Cell. Biol. 20 (3): 979-89. PMID 10629055.
Delahaye L, Rocchi S, Van Obberghen E (2000). "Potential involvement of FRS2 in insulin signaling.". Endocrinology 141 (2): 621-8. PMID 10650943.
Foehr ED, Tatavos A, Tanabe E, et al. (2000). "Discoidin domain receptor 1 (DDR1) signaling in PC12 cells: activation of juxtamembrane domains in PDGFR/DDR/TrkA chimeric receptors.". FASEB J. 14 (7): 973-81. PMID 10783152.
Wang X, Weng LP, Yu Q (2000). "Specific inhibition of FGF-induced MAPK activation by the receptor-like protein tyrosine phosphatase LAR.". Oncogene 19 (19): 2346-53. doi:10.1038/sj.onc.1203558. PMID 10822386.
Dhalluin C, Yan KS, Plotnikova O, et al. (2000). "Structural basis of SNT PTB domain interactions with distinct neurotrophic receptors.". Mol. Cell 6 (4): 921-9. PMID 11090629.
Kao S, Jaiswal RK, Kolch W, Landreth GE (2001). "Identification of the mechanisms regulating the differential activation of the mapk cascade by epidermal growth factor and nerve growth factor in PC12 cells.". J. Biol. Chem. 276 (21): 18169-77. doi:10.1074/jbc.M008870200. PMID 11278445.
Ong SH, Hadari YR, Gotoh N, et al. (2001). "Stimulation of phosphatidylinositol 3-kinase by fibroblast growth factor receptors is mediated by coordinated recruitment of multiple docking proteins.". Proc. Natl. Acad. Sci. U.S.A. 98 (11): 6074-9. doi:10.1073/pnas.111114298. PMID 11353842.
Kurokawa K, Iwashita T, Murakami H, et al. (2001). "Identification of SNT/FRS2 docking site on RET receptor tyrosine kinase and its role for signal transduction.". Oncogene 20 (16): 1929-38. doi:10.1038/sj.onc.1204290. PMID 11360177.
Melillo RM, Santoro M, Ong SH, et al. (2001). "Docking protein FRS2 links the protein tyrosine kinase RET and its oncogenic forms with the mitogen-activated protein kinase signaling cascade.". Mol. Cell. Biol. 21 (13): 4177-87. doi:10.1128/MCB.21.13.4177-4187.2001. PMID 11390647.
Hadari YR, Gotoh N, Kouhara H, et al. (2001). "Critical role for the docking-protein FRS2 alpha in FGF receptor-mediated signal transduction pathways.". Proc. Natl. Acad. Sci. U.S.A. 98 (15): 8578-83. doi:10.1073/pnas.161259898. PMID 11447289.
Yan KS, Kuti M, Yan S, et al. (2002). "FRS2 PTB domain conformation regulates interactions with divergent neurotrophic receptors.". J. Biol. Chem. 277 (19): 17088-94. doi:10.1074/jbc.M107963200. PMID 11877385.
Wong A, Lamothe B, Lee A, et al. (2002). "FRS2 alpha attenuates FGF receptor signaling by Grb2-mediated recruitment of the ubiquitin ligase Cbl.". Proc. Natl. Acad. Sci. U.S.A. 99 (10): 6684-9. doi:10.1073/pnas.052138899. PMID 11997436.
Stoletov KV, Ratcliffe KE, Terman BI (2002). "Fibroblast growth factor receptor substrate 2 participates in vascular endothelial growth factor-induced signaling.". FASEB J. 16 (10): 1283-5. doi:10.1096/fj.01-0835fje. PMID 12154000.