13
Views
122
CrossRef citations to date
0
Altmetric
Research Article

AH/PH Domain-Mediated Interaction between Akt Molecules and Its Potential Role in Akt Regulation

, , , , , , , & show all
Pages 2304-2310 | Received 13 Sep 1994, Accepted 26 Jan 1995, Published online: 30 Mar 2023

REFERENCES

  • Ahmed, N. N., T. F. Franke, A. Bellacosa, K. Datta, M. E. Gonzalez-Portal, T. Taguchi, J. R. Testa, and P. N. Tsichlis. 1993. The proteins encoded by c-akt and v-akt differ in posttranslational modification, subcellular localization and oncogenic potential. Oncogene 8:1957–1963.
  • Bellacosa, A., T. F. Franke, M. E. Gonzalez-Portal, K. Datta, T. Taguchi, J. Gardner, J. Q. Cheng, J. R. Testa, and P. N. Tsichlis. 1993. Structure, expression and chromosomal mapping of c-akt: relationship to v-akt and its implications. Oncogene 8:745–754.
  • Bellacosa, A., J. R. Testa, S. P. Staal, and P. N. Tsichlis. 1991. A retroviral oncogene, akt, encoding a serine-threonine kinase containing an SH2-like region. Science 254:274–277.
  • Benovic, J. L., A. DeBlasi, W. C. Stone, M. G. Caron, and R. J. Lefkowitz. 1989. β-Adrenergic receptor kinase: primary structure delineates a multi-gene family. Science 246:235–240.
  • Brent, R., and M. Ptashne. 1984. A bacterial repressor protein or a yeast transcriptional terminator can block upstream activation of a yeast gene. Nature (London) 312:612–615.
  • Cheng, J. Q., A. K. Godwin, A. Bellacosa, T. Taguchi, T. F. Franke, T. C. Hamilton, P. N. Tsichlis, and J. R. Testa. 1992. AKT2, a putative oncogene encoding a member of a novel subfamily of serine-threonine protein kinases, is amplified in human ovarian carcinomas. Proc. Natl. Acad. Sci. USA 89: 9267–9271.
  • Evan, G. I., G. K. Lewis, G. Ramsay, and J. M. Bishop. 1985. Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product. Mol. Cell. Biol. 5:3610–3616.
  • Fields, S., and O. Song. 1989. A novel genetic system to detect protein-protein interaction. Nature (London) 340:245–246.
  • Franke, T. F., S. Yang, T. O. Chan, K. Datta, D. K. Morrison, D. R. Kaplan, and P. N. Tsichlis. The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase. Submitted for publication.
  • Franke, T. F., K. D. Tartof, and P. N. Tsichlis. 1994. The SH2-like Akt homology (AH) domain of c-akt is present in multiple copies in the genome of vertebrate and invertebrate eucaryotes. Cloning and characterization of the Drosophila melanogaster c-akt homolog Dakt1. Oncogene 9:141–148.
  • Golemis, E. A., J. Gyuris, and R. Brent. 1994. Two hybrid systems/interaction traps, p. 13.14.1–13.14.17. In F. M. Ausubel, R. Brent, R. E. Kingston, et al. (ed.), Current protocols in molecular biology. John Wiley and Sons, New York.
  • Gyuris, J., E. A. Golemis, H. Chertkov, and R. Brent. 1993. Cdi1, a human G1 and S phase protein phosphatase that associates with Cdk2. Cell 75:791–803.
  • Ito, H., Y. Fukada, K. Murata, and A. Kimura. 1983. Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153:163–168.
  • Jones, P. F., T. Jakubowicz, and B. A. Hemmings. 1991. Molecular cloning of a second form of rac protein kinase. Cell Regul. 2:1001–1009.
  • Jones, P. F., T. Jakubowicz, F. J. Pitossi, F. Maurer, and B. A. Hemmings. 1991. Molecular cloning and identification of a serine/threonine protein kinase of the second-messenger subfamily. Proc. Natl. Acad. Sci. USA 88: 4171–4175.
  • Lefkowitz, J. L. 1993. G protein-coupled receptor kinases. Cell 74:409–412.
  • Ma, J., and M. Ptashne. 1987. A new class of yeast transcriptional activators. Cell 51:113–119.
  • Macias, M. J., A. Musacchio, H. Ponstingl, M. Nilges, M. Saraste, and H. Oschkinat. 1994. Structure of the pleckstrin homology domain from β-spec-trin. Nature (London) 369:675–677.
  • Mayer, B. J., R. Ren, K. L. Clark, and D. Baltimore. 1993. A putative modular domain present in diverse signalling proteins. Cell 73:629–630.
  • McCutchan, J. H., and J. S. Pagano. 1968. Enhancement of the infectivity of simian virus 40 deoxyribonucleic acid with diethylaminoethyl-dextran. J. Natl. Cancer Inst. 41:351–357.
  • Morgenstern, J. P., and H. Land. 1990. A series of mammalian expression vectors and characterization of their expression of a reporter gene in stably and transiently transfected cells. Nucleic Acids Res. 18:1068.
  • Morrow, J. S., and W. B. Haigh, Jr. 1983. Erythrocyte membrane proteins: detection of spectrin oligomers by gel electrophoresis. Methods Enzymol. 96:298–304.
  • Musacchio, A., T. Gibson, P. Rice, J. Thompson, and M. Saraste. 1993. The PH domain: a common piece in the structural pathwork of signalling proteins. Trends Biochem. Sci. 18:343–348.
  • Patriotis, C., A. Makris, J. Chernoff, and P. N. Tsichlis. 1994. Tpl-2 acts in concert with Ras and Raf-1 to activate mitogen-activated protein kinase. Proc. Natl. Acad. Sci. USA 91:9755–9759.
  • Rawlings, D. J., D. C. Saffran, S. Tsukada, D. A. Largaespada, J. C. Grimaldi, L. Cohen, R. N. Mohr, J. F. Bazan, M. Howard, N. G. Copeland, N. A. Jenkins, and O. N. Witte. 1993. Mutation of unique region of Bruton's tyrosine kinase in immunodeficient XID mice. Science 261:358–361.
  • Schlessinger, J., and A. Ullrich. 1992. Growth factor signaling by receptor tyrosine kinases. Neuron 9:383–391.
  • Simonds, W. F., H. K. Manjui, A. Garritsen, and A. N. Lupas. 1993. G proteins and βARK: a new twist for the coiled coil. Trends Biochem. Sci. 18:315–317.
  • Touhara, K., J. Inglese, J. A. Pitcher, G. Shaw, and R. J. Lefkowitz. 1994. Binding of G protein βγ-subunits to pleckstrin homology domains. J. Biol. Chem. 269:10217–10220.
  • Vetrie, D., I. Vorechovsky, P. Sideras, J. Holland, A. Davies, F. Flinter, L. Hammarstrom, C. Kinnon, R. Levinsky, M. Bobrow, C. I. E. Smith, and D. R. Bentley. 1993. The gene involved in X-linked agammaglobulinaemia is a member of the src family of protein-tyrosine kinases. Nature (London) 361:226–233.
  • Yoon, H. S., P. J. Hajduk, A. M. Petros, E. T. Olejniczak, R. P. Meadows, and S. W. Fesik. 1994. Solution structure of a pleckstrin-homology domain. Nature (London) 369:672–675.

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.