PTPN11
PTPN11(Protein-tyrosine phosphatase non-receptor type 11)またはSHP2(Src homology region 2 domain-containing phosphatase 2)は、ヒトではPTPN11
PTPN11はPTPファミリーに
構造 と機能
[SHP2は、パラログであるSHP1(PTPN6)と
PTPN11と関係 した遺伝子 疾患
[PTPN11
また、メタコンドロマトーシスとも
ヌーナン症候群
[ヌーナン
LEOPARD症候群
[LEPPARD
PTPN11と関係 したがん
[ヌーナン
ピロリ菌 CagAタンパク質
[ピロリ
相互 作用
[
PRPN11は
- CagA[14]
- CBL[16]
- KIT[17][18]
- CD31[19][20][21][22]
- CEACAM1[23]
- EGFR[24][25]
- Erk[26][27]
- FRS2[28][29][30]
- GAB1[31][32]
- GAB2[33][34][35][36]
- GAB3[37]
- gp130[38][39][40]
- GRB2[30][41][42][43][44][45][46][47][48]
- GHR[49][50]
- HOXA10[51]
- INSR[52][53]
- IGF1R[54][55]
- IRS1[56][57]
- JAK1[38][41]
- JAK2[41][58][59]
- LAIR1[60][61]
- LRP1[62]
- PDGFRB[63][64]
- PI3K → Akt[26]
- PLCG2[33]
- PTK2B[65]
- Ras[26][27]
- SLAMF1[66][67]
- SOCS3[38]
- SOS1[30][68]
- STAT3[13]
- STAT5A[69][70]
- STAT5B[69]
出典
[- ^ a b c GRCh38: Ensembl release 89: ENSG00000179295 - Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000043733 - Ensembl, May 2017
- ^ Human PubMed Reference:
- ^ Mouse PubMed Reference:
- ^ “Mapping a gene for Noonan syndrome to the long arm of chromosome 12”. Nat. Genet. 8 (4): 357–60. (December 1994). doi:10.1038/ng1294-357. PMID 7894486.
- ^ “Identification of a human Src homology 2-containing protein-tyrosine-phosphatase: a putative homolog of Drosophila corkscrew”. Proc. Natl. Acad. Sci. U.S.A. 89 (23): 11239–43. (December 1992). doi:10.1073/pnas.89.23.11239. PMC 50525. PMID 1280823 .
- ^ “Entrez Gene: PTPN11 protein tyrosine phosphatase, non-receptor type 11 (Noonan syndrome 1)”. 2020
年 9月 30日 閲覧 。 - ^ “Whole-genome sequencing of a single proband together with linkage analysis identifies a Mendelian disease gene”. PLoS Genet. 6 (6): e1000991. (June 2010). doi:10.1371/journal.pgen.1000991. PMC 2887469. PMID 20577567 .
- ^ “Germline gain-of-function mutations in SOS1 cause Noonan syndrome”. Nat. Genet. 39 (1): 70–4. (January 2007). doi:10.1038/ng1926. PMID 17143285.
- ^ “PTPN11 (Shp2) mutations in LEOPARD syndrome have dominant negative, not activating, effects”. J. Biol. Chem. 281 (10): 6785–92. (March 2006). doi:10.1074/jbc.M513068200. PMID 16377799.
- ^ “Activating mutations of the noonan syndrome-associated SHP2/PTPN11 gene in human solid tumors and adult acute myelogenous leukemia”. Cancer Res. 64 (24): 8816–20. (December 2004). doi:10.1158/0008-5472.CAN-04-1923. PMID 15604238.
- ^ “High NPM1 mutant allele burden at diagnosis predicts unfavorable outcomes in de novo AML”. Blood 131 (25): 2816–2825. (May 2018). doi:10.1182/blood-2018-01-828467. PMC 6265642. PMID 29724895 .
- ^ a b c “Ptpn11/Shp2 acts as a tumor suppressor in hepatocellular carcinogenesis”. Cancer Cell 19 (5): 629–39. (May 2011). doi:10.1016/j.ccr.2011.03.023. PMC 3098128. PMID 21575863 .
- ^ a b “Helicobacter pylori CagA: a new paradigm for bacterial carcinogenesis”. Cancer Science 96 (12): 835–843. (2005). doi:10.1111/j.1349-7006.2005.00130.x. PMID 16367902.
- ^ “Oncogenic mechanisms of the Helicobacter pylori CagA protein”. Nature Reviews Cancer 4 (9): 688–94. (September 2004). doi:10.1038/nrc1433. PMID 15343275.
- ^ “c-Cbl-dependent monoubiquitination and lysosomal degradation of gp130”. Mol. Cell. Biol. 28 (15): 4805–18. (Aug 2008). doi:10.1128/MCB.01784-07. PMC 2493370. PMID 18519587 .
- ^ “The ubiquitously expressed Syp phosphatase interacts with c-kit and Grb2 in hematopoietic cells”. J. Biol. Chem. 269 (40): 25206–11. (October 1994). PMID 7523381.
- ^ “SHP-1 binds and negatively modulates the c-Kit receptor by interaction with tyrosine 569 in the c-Kit juxtamembrane domain”. Mol. Cell. Biol. 18 (4): 2089–99. (April 1998). doi:10.1128/MCB.18.4.2089. PMC 121439. PMID 9528781 .
- ^ “Platelet-endothelial cell adhesion molecule-1 (CD31), a scaffolding molecule for selected catenin family members whose binding is mediated by different tyrosine and serine/threonine phosphorylation”. J. Biol. Chem. 275 (28): 21435–43. (July 2000). doi:10.1074/jbc.M001857200. PMID 10801826.
- ^ “Differential association of cytoplasmic signalling molecules SHP-1, SHP-2, SHIP and phospholipase C-gamma1 with PECAM-1/CD31”. FEBS Lett. 450 (1–2): 77–83. (April 1999). doi:10.1016/S0014-5793(99)00446-9. PMID 10350061.
- ^ “Recruitment and activation of SHP-1 protein-tyrosine phosphatase by human platelet endothelial cell adhesion molecule-1 (PECAM-1). Identification of immunoreceptor tyrosine-based inhibitory motif-like binding motifs and substrates”. J. Biol. Chem. 273 (43): 28332–40. (October 1998). doi:10.1074/jbc.273.43.28332. PMID 9774457.
- ^ “The protein-tyrosine phosphatase SHP-2 binds platelet/endothelial cell adhesion molecule-1 (PECAM-1) and forms a distinct signaling complex during platelet aggregation. Evidence for a mechanistic link between PECAM-1- and integrin-mediated cellular signaling”. J. Biol. Chem. 272 (11): 6986–93. (March 1997). doi:10.1074/jbc.272.11.6986. PMID 9054388.
- ^ “The carboxyl-terminal region of biliary glycoprotein controls its tyrosine phosphorylation and association with protein-tyrosine phosphatases SHP-1 and SHP-2 in epithelial cells”. J. Biol. Chem. 274 (1): 335–44. (Jan 1999). doi:10.1074/jbc.274.1.335. PMID 9867848.
- ^ “Phosphotyrosine interactome of the ErbB-receptor kinase family”. Mol. Syst. Biol. 1 (1): E1–E13. (2005). doi:10.1038/msb4100012. PMC 1681463. PMID 16729043 .
- ^ “Association of SH2 domain protein tyrosine phosphatases with the epidermal growth factor receptor in human tumor cells. Phosphatidic acid activates receptor dephosphorylation by PTP1C”. J. Biol. Chem. 270 (36): 21277–84. (Sep 1995). doi:10.1074/jbc.270.36.21277. PMID 7673163.
- ^ a b c L.A. Lai; C. Zhao; E.E. Zhang; G.S. Feng (2004). “14 The Shp-2 tyrosine phosphatase”. In Joaquín Ariño; Denis Alexander. Protein phosphatases. Springer. pp. 275–299. ISBN 978-3-540-20560-9
- ^ a b “The 'Shp'ing news: SH2 domain-containing tyrosine phosphatases in cell signaling”. Trends in Biochemical Sciences 28 (6): 284–293. (June 2003). doi:10.1016/S0968-0004(03)00091-4. ISSN 0968-0004. PMID 12826400.
- ^ “Potential involvement of FRS2 in insulin signaling”. Endocrinology 141 (2): 621–8. (Feb 2000). doi:10.1210/endo.141.2.7298. PMID 10650943.
- ^ “Identification of SNT/FRS2 docking site on RET receptor tyrosine kinase and its role for signal transduction”. Oncogene 20 (16): 1929–38. (Apr 2001). doi:10.1038/sj.onc.1204290. PMID 11360177.
- ^ a b c “Binding of Shp2 tyrosine phosphatase to FRS2 is essential for fibroblast growth factor-induced PC12 cell differentiation”. Mol. Cell. Biol. 18 (7): 3966–73. (Jul 1998). doi:10.1128/MCB.18.7.3966. PMC 108981. PMID 9632781 .
- ^ “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 (26): 23216–22. (Jun 2002). doi:10.1074/jbc.M200605200. PMID 11940581.
- ^ “Determination of Gab1 (Grb2-associated binder-1) interaction with insulin receptor-signaling molecules”. Mol. Endocrinol. 12 (7): 914–23. (Jul 1998). doi:10.1210/mend.12.7.0141. PMID 9658397.
- ^ a b “Phosphatidylinositol 3-kinase regulates glycosylphosphatidylinositol hydrolysis through PLC-gamma(2) activation in erythropoietin-stimulated cells”. Cell. Signal. 14 (10): 869–78. (October 2002). doi:10.1016/S0898-6568(02)00036-0. PMID 12135708.
- ^ “PKB-mediated negative feedback tightly regulates mitogenic signalling via Gab2”. EMBO J. 21 (1–2): 72–82. (January 2002). doi:10.1093/emboj/21.1.72. PMC 125816. PMID 11782427 .
- ^ “Gab2, a new pleckstrin homology domain-containing adapter protein, acts to uncouple signaling from ERK kinase to Elk-1”. J. Biol. Chem. 274 (28): 19649–54. (July 1999). doi:10.1074/jbc.274.28.19649. PMID 10391903.
- ^ “A yeast two-hybrid study of human p97/Gab2 interactions with its SH2 domain-containing binding partners”. FEBS Lett. 495 (3): 148–53. (April 2001). doi:10.1016/S0014-5793(01)02373-0. PMID 11334882.
- ^ Wolf, I.; Jenkins, B. J.; Liu, Y.; Seiffert, M.; Custodio, J. M.; Young, P.; Rohrschneider, L. R. (2002). “Gab3, a New DOS/Gab Family Member, Facilitates Macrophage Differentiation”. Molecular and Cellular Biology 22 (1): 231–244. doi:10.1128/MCB.22.1.231-244.2002. ISSN 0270-7306. PMC 134230. PMID 11739737 . "and associates transiently with the SH2 domain-containing proteins p85 and SHP2"
- ^ a b c “SHP2 and SOCS3 contribute to Tyr-759-dependent attenuation of interleukin-6 signaling through gp130”. J. Biol. Chem. 278 (1): 661–71. (January 2003). doi:10.1074/jbc.M210552200. PMID 12403768.
- ^ “Signal transduction of IL-6, leukemia-inhibitory factor, and oncostatin M: structural receptor requirements for signal attenuation”. Journal of Immunology 165 (5): 2535–43. (Sep 2000). doi:10.4049/jimmunol.165.5.2535. PMID 10946280.
- ^ “Transmembrane domain of gp130 contributes to intracellular signal transduction in hepatic cells”. J. Biol. Chem. 272 (49): 30741–7. (Dec 1997). doi:10.1074/jbc.272.49.30741. PMID 9388212.
- ^ a b c “Molecular characterization of specific interactions between SHP-2 phosphatase and JAK tyrosine kinases”. J. Biol. Chem. 272 (2): 1032–7. (January 1997). doi:10.1074/jbc.272.2.1032. PMID 8995399.
- ^ “Beta-chemokine receptor CCR5 signals through SHP1, SHP2, and Syk”. J. Biol. Chem. 275 (23): 17263–8. (Jun 2000). doi:10.1074/jbc.M000689200. PMID 10747947.
- ^ “Protein-tyrosine-phosphatase SHPTP2 couples platelet-derived growth factor receptor beta to Ras”. Proc. Natl. Acad. Sci. U.S.A. 91 (15): 7335–9. (Jul 1994). doi:10.1073/pnas.91.15.7335. PMC 44394. PMID 8041791 .
- ^ “Direct binding of Shc, Grb2, SHP-2 and p40 to the murine granulocyte colony-stimulating factor receptor”. Biochim. Biophys. Acta 1448 (1): 70–6. (Nov 1998). doi:10.1016/S0167-4889(98)00120-7. PMID 9824671.
- ^ “Induced direct binding of the adapter protein Nck to the GTPase-activating protein-associated protein p62 by epidermal growth factor”. Oncogene 15 (15): 1823–32. (Oct 1997). doi:10.1038/sj.onc.1201351. PMID 9362449.
- ^ “Fyn kinase-directed activation of SH2 domain-containing protein-tyrosine phosphatase SHP-2 by Gi protein-coupled receptors in Madin-Darby canine kidney cells”. J. Biol. Chem. 274 (18): 12401–7. (Apr 1999). doi:10.1074/jbc.274.18.12401. PMID 10212213.
- ^ “Flt3 signaling involves tyrosyl-phosphorylation of SHP-2 and SHIP and their association with Grb2 and Shc in Baf3/Flt3 cells”. J. Leukoc. Biol. 65 (3): 372–80. (Mar 1999). doi:10.1002/jlb.65.3.372. PMID 10080542.
- ^ “Epidermal growth factor induces coupling of protein-tyrosine phosphatase 1D to GRB2 via the COOH-terminal SH3 domain of GRB2”. J. Biol. Chem. 271 (35): 20981–4. (Aug 1996). doi:10.1074/jbc.271.35.20981. PMID 8702859.
- ^ “Mutation of the SHP-2 binding site in growth hormone (GH) receptor prolongs GH-promoted tyrosyl phosphorylation of GH receptor, JAK2, and STAT5B”. Mol. Endocrinol. 14 (9): 1338–50. (September 2000). doi:10.1210/me.14.9.1338. PMID 10976913.
- ^ “Grb10 identified as a potential regulator of growth hormone (GH) signaling by cloning of GH receptor target proteins”. J. Biol. Chem. 273 (26): 15906–12. (June 1998). doi:10.1074/jbc.273.26.15906. PMID 9632636.
- ^ “Constitutively active SHP2 cooperates with HoxA10 overexpression to induce acute myeloid leukemia.”. J Biol Chem 284 (4): 2549–67. (Jan 2009). doi:10.1074/jbc.M804704200. PMC 2629090. PMID 19022774 .
- ^ “Insulin receptor kinase phosphorylates protein tyrosine phosphatase containing Src homology 2 regions and modulates its PTPase activity in vitro”. Biochem. Biophys. Res. Commun. 199 (2): 780–5. (Mar 1994). doi:10.1006/bbrc.1994.1297. PMID 8135823.
- ^ “Adapter function of protein-tyrosine phosphatase 1D in insulin receptor/insulin receptor substrate-1 interaction”. J. Biol. Chem. 270 (49): 29189–93. (Dec 1995). doi:10.1074/jbc.270.49.29189. PMID 7493946.
- ^ “Concerted activity of tyrosine phosphatase SHP-2 and focal adhesion kinase in regulation of cell motility”. Mol. Cell. Biol. 19 (4): 3125–35. (Apr 1999). doi:10.1128/mcb.19.4.3125. PMC 84106. PMID 10082579 .
- ^ “Localization of the insulin-like growth factor I receptor binding sites for the SH2 domain proteins p85, Syp, and GTPase activating protein”. J. Biol. Chem. 270 (32): 19151–7. (Aug 1995). doi:10.1074/jbc.270.32.19151. PMID 7642582.
- ^ “The insulin receptor substrate 1 associates with the SH2-containing phosphotyrosine phosphatase Syp”. J. Biol. Chem. 268 (16): 11479–81. (Jun 1993). PMID 8505282.
- ^ “The COOH-terminal tyrosine phosphorylation sites on IRS-1 bind SHP-2 and negatively regulate insulin signaling”. J. Biol. Chem. 273 (41): 26908–14. (Oct 1998). doi:10.1074/jbc.273.41.26908. PMID 9756938.
- ^ “Tyrosine 425 within the activated erythropoietin receptor binds Syp, reduces the erythropoietin required for Syp tyrosine phosphorylation, and promotes mitogenesis”. Blood 87 (11): 4495–501. (June 1996). doi:10.1182/blood.V87.11.4495.bloodjournal87114495. PMID 8639815.
- ^ “SHPTP2 serves adapter protein linking between Janus kinase 2 and insulin receptor substrates”. Biochem. Biophys. Res. Commun. 228 (1): 122–7. (November 1996). doi:10.1006/bbrc.1996.1626. PMID 8912646.
- ^ “FDF03, a novel inhibitory receptor of the immunoglobulin superfamily, is expressed by human dendritic and myeloid cells”. Journal of Immunology 165 (3): 1197–209. (Aug 2000). doi:10.4049/jimmunol.165.3.1197. PMID 10903717.
- ^ “LAIR-1, a novel inhibitory receptor expressed on human mononuclear leukocytes”. Immunity 7 (2): 283–90. (Aug 1997). doi:10.1016/S1074-7613(00)80530-0. PMID 9285412.
- ^ “Structural and functional consequences of tyrosine phosphorylation in the LRP1 cytoplasmic domain”. J. Biol. Chem. 283 (23): 15656–64. (June 2008). doi:10.1074/jbc.M709514200. PMC 2414285. PMID 18381291 .
- ^ “Negative regulation of Ros receptor tyrosine kinase signaling. An epithelial function of the SH2 domain protein tyrosine phosphatase SHP-1”. J. Cell Biol. 152 (2): 325–34. (Jan 2001). doi:10.1083/jcb.152.2.325. PMC 2199605. PMID 11266449 .
- ^ “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. 268 (29): 21478–81. (Oct 1993). PMID 7691811.
- ^ “SHP2 mediates the protective effect of interleukin-6 against dexamethasone-induced apoptosis in multiple myeloma cells”. J. Biol. Chem. 275 (36): 27845–50. (September 2000). doi:10.1074/jbc.M003428200. PMID 10880513.
- ^ “Molecular dissection of the signaling and costimulatory functions of CD150 (SLAM): CD150/SAP binding and CD150-mediated costimulation”. Blood 99 (3): 957–65. (Feb 2000). doi:10.1182/blood.V99.3.957. PMID 11806999.
- ^ “Structural basis for the interaction of the free SH2 domain EAT-2 with SLAM receptors in hematopoietic cells”. EMBO J. 20 (21): 5840–52. (Nov 2001). doi:10.1093/emboj/20.21.5840. PMC 125701. PMID 11689425 .
- ^ “Erythropoietin and IL-3 induce tyrosine phosphorylation of CrkL and its association with Shc, SHP-2, and Cbl in hematopoietic cells”. Biochem. Biophys. Res. Commun. 239 (2): 412–7. (Oct 1997). doi:10.1006/bbrc.1997.7480. PMID 9344843.
- ^ a b “Cytosolic tyrosine dephosphorylation of STAT5. Potential role of SHP-2 in STAT5 regulation”. J. Biol. Chem. 275 (1): 599–604. (Jan 2000). doi:10.1074/jbc.275.1.599. PMID 10617656.
- ^ “Prolactin induces SHP-2 association with Stat5, nuclear translocation, and binding to the beta-casein gene promoter in mammary cells”. J. Biol. Chem. 277 (34): 31107–14. (Aug 2002). doi:10.1074/jbc.M200156200. PMID 12060651.
関連 文献
[- Tie-1 receptor tyrosine kinase endodomain interaction with SHP2: potential signalling mechanisms and roles in angiogenesis. Advances in Experimental Medicine and Biology. 476. (2000). 35–46. doi:10.1007/978-1-4615-4221-6_3. ISBN 978-1-4613-6895-3. PMID 10949653
- “SH2-B and SIRP: JAK2 binding proteins that modulate the actions of growth hormone.”. Recent Prog. Horm. Res. 55: 293–311. (2000). PMID 11036942.
- “Absence of PTPN11 mutations in 28 cases of cardiofaciocutaneous (CFC) syndrome”. Hum. Genet. 111 (4–5): 421–7. (2002). doi:10.1007/s00439-002-0803-6. PMID 12384786.
- “Mutations of PTPN11 are rare in adult myeloid malignancies.”. Haematologica 90 (6): 853–4. (2006). PMID 15951301.
- “Germ-line and somatic PTPN11 mutations in human disease.”. European Journal of Medical Genetics 48 (2): 81–96. (2005). doi:10.1016/j.ejmg.2005.03.001. PMID 16053901.
- “PTPN11 mutations and genotype-phenotype correlations in Noonan and LEOPARD syndromes.”. Pediatric Endocrinology Reviews : PER 2 (4): 669–74. (2006). PMID 16208280.
- “Shp2-mediated molecular signaling in control of embryonic stem cell self-renewal and differentiation.”. Cell Res. 17 (1): 37–41. (2007). doi:10.1038/sj.cr.7310140. PMID 17211446.
- “How do Shp2 mutations that oppositely influence its biochemical activity result in syndromes with overlapping symptoms?”. Cell. Mol. Life Sci. 64 (13): 1585–90. (2007). doi:10.1007/s00018-007-6509-0. PMID 17453145.