40
Views
0
CrossRef citations to date
0
Altmetric
Review

Therapeutic manipulation of the insulin receptor kinase - a review

&
Pages 191-198 | Published online: 25 Feb 2005

Bibliography

  • THEIS RS, ULLRICH A, MCCLAIN DA: Augmented mitogenesis and impaired metabolic signaling mediated by a truncated insulin receptor. J. Biol. Chem. (1989) 264:12820–12825.
  • CHAIKA OV, CHAIKA N, VOLLE DJ, WILDEN PA, PIRRUCELLO SJ, LEWIS RE: CSF-1 receptor insulin receptor chimera permits CSF-1-dependent differen-tiation of 3T3-1..1 preadipocytes. J. Biol. Chem. (1997) 272:11968–11974.
  • BOEHM JE, CHAIKA OV, LEWIS RE: Anti-apoptotic signaling by a colony-stimulating factor-1 receptor insulin receptor chimera with a uxtamembrane deletion. J. Biol. Chem. (1998) 273:7169–7176.
  • BOEHM JE, CHAIKA OV, LEWIS RE: Rac-dependent anti-apoptotic signaling by the insulin receptor cytoplasmic domain. J. Biol. Chem. (1999) 274:28632–28636.
  • CZECH MP, MASSAGUE J: Subunit structure anddynamics of the insulin receptor. Fed. Proc. (1982) 41:2719–2723.
  • ULLRICH A, BELL JR, CHEN EY et al: Human insulin receptor and its relationship to the tyrosine kinase family of oncogenes. Nature (1985) 313:756–761.
  • •One of the two first papers reporting the cloning of the insulin receptor cDNA.
  • EBINA Y, ELLIS L, JARNAGIN K et al.: The human insulin receptor cDNA: the structural basis for hormone-activated transmembrane signalling. Cell (1985) 40:747–758.
  • •One of the two first papers reporting the cloning of the insulin receptor cDNA.
  • TREADWAY JL, MORRISON BD, SOOS MA et al.: Transdominant inhibition of tyrosine kinase activity in mutant insulin/insulin-like growth Factor I hybrid receptors. Proc. Natl. Acad. ScL USA (1991) 88:214–218.
  • TORNQVIST HE, PIERCE MW, FRACKELTON AR, NEMENOFF RA, AVRUCH J: Identification of insulin receptor tyrosine residues autophosphorylated in vitro. J. Biol. Chem. (1987) 262:10212–10219.
  • TORNQVIST HE, GUNSALUS JR, NEMENOFF RA, FRACKELTON AR, AVRUCH J: Identification of the insulin receptor tyrosine residues undergoing insulin-stimulated phosphorylation in intact rat hepatoma cells. J. Biol. Chem. (1988) 263:350–359.
  • WHITE MF, LIVINGSTON JN, BACKER JM, LAURIS V, ULLRICH A, KAHN CR: Mutation of the insulin receptor at tyrosine 960 inhibits signal transmission but does not affect tyrosine kinase activity. Cell (1988) 54:641–649.
  • ECK MJ, DHE-PAGANON S, TRCJB T, NOLTE RT, SHOELSON SE: Structure of the IRS-1 PTB domain bound to the juxtamembrane region of the insulin receptor. Cell (1996) 85:695–705.
  • •A seminal paper demonstrating the structural basis for the association of the insulin receptor with an important signal-ling effector.
  • HUBBARD SR, WEI L, ELLIS L, HENDRICKSON WA: Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature (1994) 372:746–754.
  • ••The structural basis for the catalytic activity of the insulinreceptor tyrosine kinase.
  • TAKATA Y, WEBSTER NJG, OLEFSKY JM: Intracellular signaling by a mutant human insulin receptor lacking the carboxyl-terminal tyrosine autophosphorylation sites. J. Biol. Chem. (1992) 267:9065–9070.
  • PANG L, MILARSKI KL, OHMICHI M, TAKATA Y, OLEFSKY JM, SALTIEL AR: Mutation of the two carboxyl-terminal tyrosines in the insulin receptor results in enhanced activation of mitogen-activated protein kinase. J. Biol. Chem. (1994) 269:10604–10608.
  • FUJITA-YAMAGUCHI Y, SACKS DB, MCDONALD JM, SAHAL D, KATHURIA S: Effect of basic polycations and proteins on purified insulin receptor. Insulin-independent activation of the receptor tyrosine-specific protein kinase by poly(L-lysine). J. Biol. Chem. (1989) 263:813–822.
  • MORRISON BD, FELTZ SM, PESSIN JE: Polylysine specifi-cally activates the insulin-dependent insulin receptor protein kinase. J. Biol. Chem. (1989) 264:9994–10001.
  • ROSEN OM, HERRERA R, OLOWE Y, PETTRUZZELLI LM, COBB MH: Phosphorylation activates the insulin receptor tyrosine protein kinase. Proc. Natl. Acad. ScL USA (1983) 80:3237–3240.
  • YU K-T, CZECH MP: Tyrosine phosphorylation of the insulin receptor 13 subunit activates the receptor-associated tyrosine kinase activity. J. Biol. Chem. (1984) 259:5277–5286.
  • JACOBS S, SAHYOUN NE, SALTIEL AR, CUATRECASAS P: Phorbol esters stimulate the phosphorylation of receptors for insulin and somatomedin C. Proc. Natl. Acad. ScL USA (1983) 80:6211–6213.
  • TAKAYAMA S, WHITE MF, LAURIS V, KAHN CR: Phorbol ester-induced serine phosphorylation of the insulin receptor decreases its tyrosine kinase activity. J. Biol. Chem. (1988) 81:7797–7801.
  • KADOTA S, FANTUS IG, GGUYDA HJ, POSNER BI: Stimulation of insulin-like growth Factor II receptor binding and insulin receptor kinase activity in rat adipocytes. Effects of vanadate and 11202.1 Biol. Chem. (1987) 262:8252–8256.
  • POSNER BI, FAURE R, BURGESS JAN et al.: Peroxovana-dium compounds. A new class of potent phosphotyrosine phosphatase inhibitors which are insulin mimetics. J. Biol. Chem. (1994) 269:4596–4604.
  • BOLLAG GE, ROTH RA, BEAUDOIN J, MOCHLY-ROSEN D,KOSHLAND JRDE: Protein kinase C directly phosphory-lates the insulin receptor in vitro and reduces its protein-tyrosine kinase activity. Biochemistry (1986) 83:5822–5824.
  • LEVITZKI A, GAZIT A: Tyrosine kinase inhibition: anapproach to drug development. Science (1995) 267:1782–1788.
  • •A thorough review of tyrosine kinase inhibition.
  • MADDUX BA, SBRACCIA P, KUMAKURA S et al. Membrane glycoprotein PC-1 and insulin resistance in non-insulin-dependent diabetes mellitus. Nature (1995) 373:448–451.
  • BACKER JM, KAHN CR, CAHILL DA, ULLRICH A, WHITEMF: Receptor-mediated internalization of insulin requires a 12-amino acid sequence in the juxtamem-brane region of the insulin receptor 6-subunit. J. Biol. Chem. (1990) 265:16450–16454.
  • MCCLAIN DA: Mechanism and role of insulin receptorendocytosis. Am. J. Med. ScL (1992) 304:192–201.
  • KNUTSON VP, DONNELLY PV, BALBA Y, LOPEZ-REYES M:Insulin resistance is mediated by a proteolytic fragment of the insulin receptor. J. Biol. Chem. (1995) 270:24972–24981.
  • YENUSH L, WHITE MF: The IRS-signalling systemduring insulin and cytokine action. Bio Essays (1997) 19:491–500.
  • STAUBS PA, REICHART DR, SALTIEL AR et al.: Localizationof the insulin receptor binding sites for the S112 domain proteins p85, Syp, and GAP. J. Biol. Chem. (1994) 269:27186–27192.
  • O'NEILL TJ, ROSE DW, PILLAY TS, HOTTA K, OLEFSKY JM,GUSTAFSON TA: Interaction of a GRB-IR splice variant (a human GRB10 homolog) with the insulin and insulin-like growth Factor I receptors - evidence for a role in mitogenic signaling. J. Biol. Chem. (1996) 271:22506–22513.
  • LIU F, ROTH RA: Grb-IR: A S112-domain-containingprotein that binds to the insulin receptor and inhibits its function. Proc. Natl. Acad. ScL USA (1995) 92:10287–10291.
  • FRANTZ JD, GIORGETTI-PERALDI S, OTTINGER EA,SHOELSON SE: Human GRB-1R13 /GRB10 - splice variants of an insulin and growth factor receptor-binding protein with PH and S112 domains. J. Biol. Chem. (1997) 272:2659–2667.
  • FAMBROUGH D, MCCLURE K, KAZLAUSKAS A, LANDER ES: Diverse signaling pathways activated by growth factor receptors induce broadly overlapping, rather than independent, sets of genes. Cell (1999) 11:727–741.
  • ••A seminal demonstration of the use of DNA microarrays todissect growth factor receptor-mediated effects on gene expression.
  • SHARMA PM, EGAWA K, GUSTAFSON TA, MARTIN JL, OLEFSKY JM: Adenovirus-mediated overexpression of IRS-1 interacting domains abolishes insulin-stimulated mitogenesis without affecting glucose transport in 3T3-L1 adipocytes. Mol Cell Biol. (1997) 17:7386–7397.
  • IMAMURA T, VOLLENWEIDER P, EGAWA K et al.: G a-q/11protein plays a key role in insulin-induced glucose transport in 3T3-L1 adipocytes. Mol. Cell Biol. (1999) 19:6765–6774.
  • YENUSH L, ZANELLA C, UCHIDA T, BERNAL D, WHITE MF:The pleckstrin homology and phosphotyrosine binding domains of insulin receptor substrate 1 mediate inhibition of apoptosis by insulin. Mol. Biol. (1998) 18:6784–6794.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.