Sprouty homolog 2 (Drosophila), also known as SPRY2, is a human gene.

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summary_text = This gene encodes a protein belonging to the sprouty family. The encoded protein contains a carboxyl-terminal cysteine-rich domain essential for the inhibitory activity on receptor tyrosine kinase signaling proteins and is required for growth factor stimulated translocation of the protein to membrane ruffles. In primary dermal endothelial cells this gene is transiently upregulated in response to fibroblast growth factor two. This protein is indirectly involved in the non-cell autonomous inhibitory effect on fibroblast growth factor two signaling. The protein interacts with Cas-Br-M (murine) ectropic retroviral transforming sequence, and can function as a bimodal regulator of epidermal growth factor receptor/mitogen-activated protein kinase signaling. This protein may play a role in alveoli branching during lung development as shown by a similar mouse protein.cite web | title = Entrez Gene: SPRY2 sprouty homolog 2 (Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10253| accessdate = ]


Further reading

citations =
*cite journal | author=Hacohen N, Kramer S, Sutherland D, "et al." |title=sprouty encodes a novel antagonist of FGF signaling that patterns apical branching of the Drosophila airways. |journal=Cell |volume=92 |issue= 2 |pages= 253–63 |year= 1998 |pmid= 9458049 |doi=
*cite journal | author=Lim J, Wong ES, Ong SH, "et al." |title=Sprouty proteins are targeted to membrane ruffles upon growth factor receptor tyrosine kinase activation. Identification of a novel translocation domain. |journal=J. Biol. Chem. |volume=275 |issue= 42 |pages= 32837–45 |year= 2000 |pmid= 10887178 |doi= 10.1074/jbc.M002156200
*cite journal | author=Glienke J, Fenten G, Seemann M, "et al." |title=Human SPRY2 inhibits FGF2 signalling by a secreted factor. |journal=Mech. Dev. |volume=96 |issue= 1 |pages= 91–9 |year= 2000 |pmid= 10940627 |doi=
*cite journal | author=Wong ES, Lim J, Low BC, "et al." |title=Evidence for direct interaction between Sprouty and Cbl. |journal=J. Biol. Chem. |volume=276 |issue= 8 |pages= 5866–75 |year= 2001 |pmid= 11053437 |doi= 10.1074/jbc.M006945200
*cite journal | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788–95 |year= 2001 |pmid= 11076863 |doi=
*cite journal | author=Wiemann S, Weil B, Wellenreuther R, "et al." |title=Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. |journal=Genome Res. |volume=11 |issue= 3 |pages= 422–35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.154701
*cite journal | author=Yusoff P, Lao DH, Ong SH, "et al." |title=Sprouty2 inhibits the Ras/MAP kinase pathway by inhibiting the activation of Raf. |journal=J. Biol. Chem. |volume=277 |issue= 5 |pages= 3195–201 |year= 2002 |pmid= 11698404 |doi= 10.1074/jbc.M108368200
*cite journal | author=Egan JE, Hall AB, Yatsula BA, Bar-Sagi D |title=The bimodal regulation of epidermal growth factor signaling by human Sprouty proteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 9 |pages= 6041–6 |year= 2002 |pmid= 11983899 |doi= 10.1073/pnas.052090899
*cite journal | author=Wong ES, Fong CW, Lim J, "et al." |title=Sprouty2 attenuates epidermal growth factor receptor ubiquitylation and endocytosis, and consequently enhances Ras/ERK signalling. |journal=EMBO J. |volume=21 |issue= 18 |pages= 4796–808 |year= 2002 |pmid= 12234920 |doi=
*cite journal | author=Lim J, Yusoff P, Wong ES, "et al." |title=The cysteine-rich sprouty translocation domain targets mitogen-activated protein kinase inhibitory proteins to phosphatidylinositol 4,5-bisphosphate in plasma membranes. |journal=Mol. Cell. Biol. |volume=22 |issue= 22 |pages= 7953–66 |year= 2002 |pmid= 12391162 |doi=
*cite journal | author=Hanafusa H, Torii S, Yasunaga T, Nishida E |title=Sprouty1 and Sprouty2 provide a control mechanism for the Ras/MAPK signalling pathway. |journal=Nat. Cell Biol. |volume=4 |issue= 11 |pages= 850–8 |year= 2004 |pmid= 12402043 |doi= 10.1038/ncb867
*cite journal | author=Yigzaw Y, Poppleton HM, Sreejayan N, "et al." |title=Protein-tyrosine phosphatase-1B (PTP1B) mediates the anti-migratory actions of Sprouty. |journal=J. Biol. Chem. |volume=278 |issue= 1 |pages= 284–8 |year= 2003 |pmid= 12414790 |doi= 10.1074/jbc.M210359200
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Hall AB, Jura N, DaSilva J, "et al." |title=hSpry2 is targeted to the ubiquitin-dependent proteasome pathway by c-Cbl. |journal=Curr. Biol. |volume=13 |issue= 4 |pages= 308–14 |year= 2003 |pmid= 12593796 |doi=
*cite journal | author=Sasaki A, Taketomi T, Kato R, "et al." |title=Mammalian Sprouty4 suppresses Ras-independent ERK activation by binding to Raf1. |journal=Nat. Cell Biol. |volume=5 |issue= 5 |pages= 427–32 |year= 2003 |pmid= 12717443 |doi= 10.1038/ncb978
*cite journal | author=Fong CW, Leong HF, Wong ES, "et al." |title=Tyrosine phosphorylation of Sprouty2 enhances its interaction with c-Cbl and is crucial for its function. |journal=J. Biol. Chem. |volume=278 |issue= 35 |pages= 33456–64 |year= 2003 |pmid= 12815057 |doi= 10.1074/jbc.M301317200
*cite journal | author=Hanafusa H, Torii S, Yasunaga T, "et al." |title=Shp2, an SH2-containing protein-tyrosine phosphatase, positively regulates receptor tyrosine kinase signaling by dephosphorylating and inactivating the inhibitor Sprouty. |journal=J. Biol. Chem. |volume=279 |issue= 22 |pages= 22992–5 |year= 2004 |pmid= 15031289 |doi= 10.1074/jbc.M312498200
*cite journal | author=Dunham A, Matthews LH, Burton J, "et al." |title=The DNA sequence and analysis of human chromosome 13. |journal=Nature |volume=428 |issue= 6982 |pages= 522–8 |year= 2004 |pmid= 15057823 |doi= 10.1038/nature02379
*cite journal | author=Lee CC, Putnam AJ, Miranti CK, "et al." |title=Overexpression of sprouty 2 inhibits HGF/SF-mediated cell growth, invasion, migration, and cytokinesis. |journal=Oncogene |volume=23 |issue= 30 |pages= 5193–202 |year= 2004 |pmid= 15122328 |doi= 10.1038/sj.onc.1207646
*cite journal | author=Chi L, Zhang S, Lin Y, "et al." |title=Sprouty proteins regulate ureteric branching by coordinating reciprocal epithelial Wnt11, mesenchymal Gdnf and stromal Fgf7 signalling during kidney development. |journal=Development |volume=131 |issue= 14 |pages= 3345–56 |year= 2004 |pmid= 15201220 |doi= 10.1242/dev.01200

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  • SPRY1 — Sprouty homolog 1, antagonist of FGF signaling (Drosophila), also known as SPRY1, is a human gene.cite web | title = Entrez Gene: SPRY1 sprouty homolog 1, antagonist of FGF signaling (Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db …   Wikipedia

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