Src tyrosine kinase regulates insulin-induced activation of protein kinase C (PKC) δ in skeletal muscle

Cellular Signalling

Volumn 16, Issue 11, 2004, Pages 1299-1308

  Rosenzweig, Tovit ^a   Aga Mizrachi, Shlomit ^a   Bak, Asia ^a   Sampson, Sanford R ^a  

^a BAR ILAN UNIVERSITY   (Israel)

Author keywords

Glucose uptake; PKC; Skeletal muscle; Tyrosine kinase; Tyrosine phosphorylation

Indexed keywords

INSULIN; PROTEIN KINASE C DELTA; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE KINASE INHIBITOR;

ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVITY; GLUCOSE TRANSPORT; INFRARED RADIATION; MOUSE; NEWBORN; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; SKELETAL MUSCLE;

ANIMALS; ANIMALS, NEWBORN; CELLS, CULTURED; ENZYME ACTIVATION; ENZYME INHIBITORS; GLUCOSE; INSULIN; MICE; MUSCLE, SKELETAL; PHOSPHORYLATION; PROTEIN KINASE C; PROTEIN KINASE C-DELTA; PYRIMIDINES; RECEPTOR, INSULIN; SIGNAL TRANSDUCTION; SRC-FAMILY KINASES; TYROSINE;

EID: 4444233869     PISSN: 08986568     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cellsig.2004.03.015     Document Type: Article

References (32)

1. White M.F., Kahn C.R. The insulin signaling system. J. Biol. Chem. 269:1994;1-4
2. Braiman L., Sheffi-Friedman L., Bak A., Tennenbaum T., Sampson S.R. Tyrosine phosphorylation of specific protein kinase C isoenzymes participates in insulin stimulation of glucose transport in primary cultures of rat skeletal muscle. Diabetes. 48:1999;1922-1929
3. Braiman L., Alt A., Kuroki T., Ohba M., Bak A., Tennenbaum T., Sampson S.R. Protein kinase Cdelta mediates insulin-induced glucose transport in primary cultures of rat skeletal muscle. Mol. Endocrinol. 13:1999;2002-2012
4. Braiman L., Alt A., Kuroki T., Ohba M., Bak A., Tennenbaum T., Sampson S.R. Insulin induces specific interaction between insulin receptor and PKC in primary cultured skeletal muscle. Mol. Endocrinol. 15:2001;565-574
5. Rosenzweig T., Braiman L., Bak A., Alt A., Kuroki T., Sampson S.R. Differential effects of tumor necrosis factor-alpha on protein kinase C isoforms alpha and delta mediate inhibition of insulin receptor signaling. Diabetes. 51:2002;1921-1930
6. Li W., Mischak H., Yu J.C., Wang L.M., Mushinski J.F., Heidaran M.A., Pierce J.H. Tyrosine phosphorylation of protein kinase C-δ in response to its activation. J. Biol. Chem. 269:1994;2349-2352
7. Denning M.F., Dlugosz A.A., Threadgill D.W., Maguson T., Yuspa S.H. Activation of the epidermal growth factor receptor signal transduction pathway stimulates tyrosine phosphorylation of protein kinase C. J. Biol. Chem. 271:1996;5325-5331
8. Kassenbrock C.K., Hunter S., Garl P., Johnson G.L., Anderson S.M. Inhibition of Src family kinases blocks EGF-induced activation of Akt, phosphorylation of c-Cbl, and ubiquitination of the EGF receptor. J. Biol. Chem. 2002;24967-24975
9. Song J.S., Swann P.G., Szallasi Z., Blank U., Blumberg P.M., Rivera J. Tyrosine phosphorylation-dependent and -independent associations of protein kinase C-delta with Src family kinases in the RBL-2H3 mast cell line: regulation of Src family kinase activity by protein kinase C-delta. Oncogene. 16:1998;3357-3368
10. Gschwendt M., Kielbassa K., Kittstein W., Marks F. Tyrosine phosphorylation and stimulation of protein kinase Cδ from porcine spleen by Src in vitro. Dependence on the activated state of protein kinase Cδ FEBS Lett. 347:1994;85-89
11. Kikkawa U., Matsuzaki H., Yamamoto T. Protein kinase Cdelta (PKCdelta): activation mechanisms and functions. J. Biochem. (Tokyo). 132:2002;831-839
12. Arbet-Engels C., Tartare-Deckert S., Eckhart W. C-terminal Src kinase associates with ligand-stimulated insulin-like growth factor-I receptor. J. Biol. Chem. 274:1999;5422-5428
13. Li W., Jiang Y.X., Zhang J., Soon L., Flechner L., Kapoor V., Pierce J.H., Wang L.H. Protein kinase C-delta is an important signaling molecule in insulin-like growth factor I receptor-mediated cell transformation. Mol. Cell. Biol. 18:1998;5888-5898
14. Benes C., Soltoff S.P. Modulation of PKCdelta tyrosine phosphorylation and activity in salivary and PC-12 cells by Src kinases. Am. J. Physiol., Cell Physiol. 280:2001;C1498-C1510
15. Yu K.T., Werth D.K., Pastan I.H., Czech M.P. Src kinase catalyzes the phosphorylation and activation of the insulin receptor kinase. J. Biol. Chem. 260:1985;5838-5846
16. Brodie C., Bak A., Shainberg A., Sampson S.R. Role of Na-K ATPase in regulation of resting membrane potential of cultured rat skeletal myotubes. J. Cell. Physiol. 130:1987;191-198
17. Brodie C., Brody M., Sampson S.R. Characterization of the relation between sodium channels and electrical activity in cultured rat skeletal myotubes: regulatory aspects. Brain Res. 488:1989;186-194
18. Vigdor-Alboim S., Rothman C., Braiman L., Bak A., Langzam L., Yosef O., Sterengarz B.B., Nawrath H., Brodie C., Sampson S.R. Discoordinate regulation of different K channels in cultured rat skeletal muscle by nerve growth factor. J. Neurosci. Res. 56:1999;275-283
19. Sampson S.R., Brodie C., Alboim S.V. Role of protein kinase C in insulin activation of the Na-K pump in cultured skeletal muscle. Am. J. Physiol. 266:1994;C751-C758
20. Cheng A., Bal G.S., Kennedy B.P., Tremblay M.L. Attenuation of adhesion-dependent signaling and cell spreading in transformed fibroblasts lacking protein tyrosine phosphatase-1B. J. Biol. Chem. 276(28):2001 (Jul. 13);25848-25855
21. Bjorge J.D., Pang A., Fujita D.J. Identification of protein-tyrosine phosphatase 1B as the major tyrosine phosphatase activity capable of dephosphorylating and activating c-Src in several human breast cancer cell lines. J. Biol. Chem. 275(52):2000 (Dec. 29);41439-41446
22. Shumay E., Song X., Wang H.Y., Malbon C.C. pp60Src mediates insulin-stimulated sequestration of the beta(2)-adrenergic receptor: insulin stimulates pp60Src phosphorylation and activation. Mol. Biol. Cell. 13:2002;3943-3954
23. Boney C.M., Sekimoto H., Gruppuso P.A., Frackelton A.R. Jr. Src family tyrosine kinases participate in insulin-like growth factor I mitogenic signaling in 3T3-L1 cells. Cell Growth Differ. 12:2001;379-386
24. Vandenplas M.L., Mouton W.L., Vandenplas S., Bester A.J., Ricketts M.H. Increased intracellular Ca2+ is necessary for maximal expression of the proto-oncogene c-Jun in the Jurkat T-cell line. Biochem. J. 267:1990;349-351
25. Stephens L.R., Anderson K.E., Hawkins P.T. Src family kinases mediate receptor-stimulated, phosphoinositide 3-kinase-dependent, tyrosine phosphorylation of dual adaptor for phosphotyrosine and 3-phosphoinositides-1 in endothelial and B cell lines. J. Biol. Chem. 276:2001;42767-42773
26. Kaburagi Y., Satoh S., Tamemoto H., Yamamoto-Honda R., Tobe K., Veki K., Yamauchi T., Kono-Sugita E., Sekihara H., Aizawa S., Cushman S.W., Akanuma Y., Yazaki Y., Kadowaki T. Role of insulin receptor substrate-1 and pp60 in the regulation of insulin-induced glucose transport and GLUT4 translocation in primary adipocytes. J. Biol. Chem. 272:1997;25839-25844
27. Cheatham B., Kahn C.R. Insulin action and the insulin signaling network. Endocr. Rev. 16:1995;117-142
28. Myers M.G.J., Grammer T.C., Wang L.M., Sun X.J., Pierce J.H., Blenis J., White M.F. Insulin receptor substrate-1 mediates phosphatidylinositol 3′-kinase and p70S6k signaling during insulin, insulin-like growth factor-1, and interleukin-4 stimulation. J. Biol. Chem. 269:1994;28783-28789
29. Myers M.G.J., Sun X.J., Cheatham B., Jachna B.R., Glasheen E.M., Backer J.M., White M.F. IRS-1 is a common element in insulin and insulin-like growth factor-I signaling to the phosphatidylinositol 3′-kinase. Endocrinology. 132:1993;1421-1430
30. White M.F. The insulin signalling system and the IRS proteins. Diabetologia. 40(Suppl. 2):1997;S2-S17
31. Kronfeld I., Kazimirsky G., Lorenzo P.S., Garfield S.H., Blumberg P.M., Brodie C. Phosphorylation of protein kinase Cdelta on distinct tyrosine residues regulates specific cellular functions. J. Biol. Chem. 275:2000;35491-35498
32. Zang Q., Lu Z., Curto M., Barile N., Shalloway D., Foster D.A. Association between v-Src and protein kinase C delta in v-Src-transformed fibroblasts. J. Biol. Chem. 272:1997;13275-13280