SPRY2

From Wikipedia, the free encyclopedia


Sprouty homolog 2 (Drosophila)
Identifiers
Symbol(s) SPRY2; MGC23039; hSPRY2
External IDs OMIM: 602466 MGI1345138 HomoloGene4267
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 10253 24064
Ensembl ENSG00000136158 ENSMUSG00000022114
Uniprot O43597 Q9QXV8
Refseq NM_005842 (mRNA)
NP_005833 (protein)
NM_011897 (mRNA)
NP_036027 (protein)
Location Chr 13: 79.81 - 79.81 Mb Chr 14: 104.78 - 104.78 Mb
Pubmed search [1] [2]

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

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.[1]

[edit] References

[edit] Further reading

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