메뉴 건너뛰기




Volumn 287, Issue 4, 2012, Pages 2423-2436

Novel mechanistic link between focal adhesion remodeling and glucose-stimulated insulin secretion

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN CYTOSKELETON; BASAL CELLS; CELL FUNCTIONS; CELL SURFACES; CLOSE PROXIMITY; COLOCALIZATION; EXTRACELLULAR MATRICES; F-ACTIN; FOCAL ADHESION KINASE; FOCAL ADHESIONS; GLUCOSE-RESPONSIVE; GLUCOSE-STIMULATED INSULIN SECRETIONS; INSULIN GRANULES; INSULIN SECRETION; INTEGRINS; INTRACELLULAR SIGNALING; MECHANISTIC LINK; PAXILLIN; PHARMACOLOGICAL INHIBITION; SHORT TERM; SIGNALING PATHWAYS; TOTAL INTERNAL REFLECTION FLUORESCENCE MICROSCOPY;

EID: 84856074212     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.279885     Document Type: Article
Times cited : (64)

References (81)
  • 1
    • 0021187646 scopus 로고
    • +channels in pancreatic B cells
    • +channels in pancreatic B cells. Nature 311, 271-273
    • (1984) Nature , vol.311 , pp. 271-273
    • Cook, D.L.1    Hales, C.N.2
  • 2
    • 0021741559 scopus 로고
    • Glucose induces closure of single potassium channels in isolated rat pancreatic β-cells
    • DOI 10.1038/312446a0
    • Ashcroft, F. M., Harrison, D. E., and Ashcroft, S. J. (1984) Glucose induces closure of single potassium channels in isolated rat pancreatic β Cells. Nature 312, 446-448 (Pubitemid 15217837)
    • (1984) Nature , vol.312 , Issue.5993 , pp. 446-448
    • Ashcroft, F.M.1    Harrison, D.E.2    Ashcroft, S.J.H.3
  • 4
    • 0022467904 scopus 로고
    • Pancreatic islet glucose metabolism and regulation of insulin secretion
    • Meglasson, M. D., and Matschinsky, F. M. (1986) Pancreatic islet glucose metabolism and regulation of insulin secretion. Diabetes Metab. Rev. 2, 163-214 (Pubitemid 16009507)
    • (1986) Diabetes/Metabolism Reviews , vol.2 , Issue.3-4 , pp. 163-214
    • Meglasson, M.D.1    Matschinsky, F.M.2
  • 5
    • 0023525741 scopus 로고
    • 2+, cAMP, and phospholipid-derived messengers in coupling mechanisms of insulin secretion
    • 2+, cAMP, and phospholipid-derived messengers in coupling mechanisms of insulin secretion. Physiol. Rev. 67, 1185-1248
    • (1987) Physiol. Rev. , vol.67 , pp. 1185-1248
    • Prentki, M.1    Matschinsky, F.M.2
  • 6
    • 64149126546 scopus 로고    scopus 로고
    • Regulation of insulin secretion. A matter of phase control and amplitude modulation
    • Henquin, J. C. (2009) Regulation of insulin secretion. A matter of phase control and amplitude modulation. Diabetologia 52, 739-751
    • (2009) Diabetologia , vol.52 , pp. 739-751
    • Henquin, J.C.1
  • 7
    • 0014336473 scopus 로고
    • Dynamics of insulin secretion by the perfused rat pancreas
    • Curry, D. L., Bennett, L. L., and Grodsky, G. M. (1968) Dynamics of insulin secretion by the perfused rat pancreas. Endocrinology 83, 572-584
    • (1968) Endocrinology , vol.83 , pp. 572-584
    • Curry, D.L.1    Bennett, L.L.2    Grodsky, G.M.3
  • 9
    • 0019013375 scopus 로고
    • Comparison of storage- and signal-limited models of pancreatic insulin secretion
    • O'Connor, M. D., Landahl, H., and Grodsky, G. M. (1980) Comparison of storage- and signal-limited models of pancreatic insulin secretion. Am. J. Physiol. 238, R378-R389
    • (1980) Am. J. Physiol. , vol.238
    • O'Connor, M.D.1    Landahl, H.2    Grodsky, G.M.3
  • 10
    • 0042879951 scopus 로고    scopus 로고
    • Insulin granule dynamics in pancreatic beta cells
    • DOI 10.1007/s00125-003-1153-1
    • Rorsman, P., and Renström, E. (2003) Insulin granule dynamics in pancreatic β cells. Diabetologia 46, 1029-1045 (Pubitemid 37041234)
    • (2003) Diabetologia , vol.46 , Issue.8 , pp. 1029-1045
    • Rorsman, P.1    Renstrom, E.2
  • 14
    • 0030022630 scopus 로고    scopus 로고
    • Expression and functional role of syntaxin 1/HPC-1 in pancreatic β cells. Syntaxin 1A, but not 1B, plays a negative role in regulatory insulin release pathway
    • Nagamatsu, S., Fujiwara, T., Nakamichi, Y., Watanabe, T., Katahira, H., Sawa, H., and Akagawa, K. (1996) Expression and functional role of syntaxin 1/HPC-1 in pancreatic β cells. Syntaxin 1A, but not 1B, plays a negative role in regulatory insulin release pathway. J. Biol. Chem. 271, 1160-1165
    • (1996) J. Biol. Chem. , vol.271 , pp. 1160-1165
    • Nagamatsu, S.1    Fujiwara, T.2    Nakamichi, Y.3    Watanabe, T.4    Katahira, H.5    Sawa, H.6    Akagawa, K.7
  • 16
    • 0018755463 scopus 로고
    • Interaction between insulin-storage granules and F-actin in vitro
    • Howell, S. L., and Tyhurst, M. (1979) Interaction between insulin storage granules and F-actin in vitro. Biochem. J. 178, 367-371 (Pubitemid 9152301)
    • (1979) Biochemical Journal , vol.178 , Issue.2 , pp. 367-371
    • Howell, S.L.1    Tyhurst, M.2
  • 17
    • 0015500457 scopus 로고
    • Pancreatic β cell web. Its possible role in insulin secretion
    • Orci, L., Gabbay, K. H., and Malaisse, W. J. (1972) Pancreatic β cell web. Its possible role in insulin secretion. Science 175, 1128-1130
    • (1972) Science , vol.175 , pp. 1128-1130
    • Orci, L.1    Gabbay, K.H.2    Malaisse, W.J.3
  • 18
    • 0018409526 scopus 로고
    • Motile events in pancreatic endocrine cells
    • Somers, G., Blondel, B., Orci, L., and Malaisse, W. J. (1979) Motile events in pancreatic endocrine cells. Endocrinology 104, 255-264 (Pubitemid 9093335)
    • (1979) Endocrinology , vol.104 , Issue.1 , pp. 255-264
    • Somers, G.1    Blondel, B.2    Orci, L.3    Malaisse, W.J.4
  • 20
    • 0041887212 scopus 로고    scopus 로고
    • Glucose regulates the cortical actin network through modulation of Cdc42 cycling to stimulate insulin secretion
    • Nevins, A. K., and Thurmond, D. C. (2003) Glucose regulates the cortical actin network through modulation of Cdc42 cycling to stimulate insulin secretion. Am. J. Physiol. Cell Physiol. 285, C698-C710 (Pubitemid 37022068)
    • (2003) American Journal of Physiology - Cell Physiology , vol.285 , Issue.3
    • Nevins, A.K.1    Thurmond, D.C.2
  • 21
    • 0037384072 scopus 로고    scopus 로고
    • Glucose-stimulated insulin secretion is coupled to the interaction of actin with the t-SNARE (target membrane soluble N-ethylmaleimide-sensitive factor attachment protein receptor protein) complex
    • DOI 10.1210/me.2002-0333
    • Thurmond, D. C., Gonelle-Gispert, C., Furukawa, M., Halban, P. A., and Pessin, J. E. (2003) Glucose-stimulated insulin secretion is coupled to the interaction of actin with the t-SNARE (target membrane soluble N-ethylmaleimide-sensitive factor attachment protein receptor protein) complex. Mol. Endocrinol. 17, 732-742 (Pubitemid 36403583)
    • (2003) Molecular Endocrinology , vol.17 , Issue.4 , pp. 732-742
    • Thurmond, D.C.1    Gonelle-Gispert, C.2    Furukawa, M.3    Halban, P.A.4    Pessin, J.E.5
  • 22
    • 33745201223 scopus 로고    scopus 로고
    • Regulation of pancreatic β-cell insulin secretion by actin cytoskeleton remodelling: Role of gelsolin and cooperation with the MAPK signalling pathway
    • DOI 10.1242/jcs.02942
    • Tomas, A., Yermen, B., Min, L., Pessin, J. E., and Halban, P. A. (2006) Regulation of pancreatic β cell insulin secretion by actin cytoskeleton remodeling. Role of gelsolin and cooperation with the MAPK signaling pathway. J. Cell Sci. 119, 2156-2167 (Pubitemid 43904970)
    • (2006) Journal of Cell Science , vol.119 , Issue.10 , pp. 2156-2167
    • Tomas, A.1    Yermen, B.2    Min, L.3    Pessin, J.E.4    Halban, P.A.5
  • 23
    • 65649089183 scopus 로고    scopus 로고
    • Integrins in cell migration. The actin connection
    • Vicente-Manzanares, M., Choi, C. K., and Horwitz, A. R. (2009) Integrins in cell migration. The actin connection. J. Cell Sci. 122, 199-206
    • (2009) J. Cell Sci. , vol.122 , pp. 199-206
    • Vicente-Manzanares, M.1    Choi, C.K.2    Horwitz, A.R.3
  • 24
    • 0028817908 scopus 로고
    • Convergence of integrin and growth factor receptor signaling pathways within the focal adhesion complex
    • Plopper, G. E., McNamee, H. P., Dike, L. E., Bojanowski, K., and Ingber, D. E. (1995) Convergence of integrin and growth factor receptor signaling pathways within the focal adhesion complex. Mol. Biol. Cell 6, 1349-1365
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1349-1365
    • Plopper, G.E.1    McNamee, H.P.2    Dike, L.E.3    Bojanowski, K.4    Ingber, D.E.5
  • 26
    • 0027459771 scopus 로고
    • Signal transduction from the extracellular matrix
    • DOI 10.1083/jcb.120.3.577
    • Juliano, R. L., and Haskill, S. (1993) Signal transduction from the extracellular matrix. J. Cell Biol. 120, 577-585 (Pubitemid 23035126)
    • (1993) Journal of Cell Biology , vol.120 , Issue.3 , pp. 577-585
    • Juliano, R.L.1    Haskill, S.2
  • 27
    • 79953171148 scopus 로고    scopus 로고
    • Focal adhesion remodeling is crucial for glucose-stimulated insulin secretion and involves activation of focal adhesion kinase and paxillin
    • Rondas, D., Tomas, A., and Halban, P. A. (2011) Focal adhesion remodeling is crucial for glucose-stimulated insulin secretion and involves activation of focal adhesion kinase and paxillin. Diabetes 60, 1146-1157
    • (2011) Diabetes , vol.60 , pp. 1146-1157
    • Rondas, D.1    Tomas, A.2    Halban, P.A.3
  • 28
    • 0037390423 scopus 로고    scopus 로고
    • Differential gene expression in well-regulated and dysregulated pancreatic β-cell (MIN6) sublines
    • DOI 10.1210/en.2002-220916
    • Lilla, V., Webb, G., Rickenbach, K., Maturana, A., Steiner, D. F., Halban, P. A., and Irminger, J. C. (2003) Differential gene expression in well regulated and dysregulated pancreatic β cell (MIN6) sublines. Endocrinology 144, 1368-1379 (Pubitemid 36428479)
    • (2003) Endocrinology , vol.144 , Issue.4 , pp. 1368-1379
    • Lilla, V.1    Webb, G.2    Rickenbach, K.3    Maturana, A.4    Steiner, D.F.5    Halban, P.A.6    Irminger, J.-C.7
  • 29
    • 0033969520 scopus 로고    scopus 로고
    • Importance of cell-matrix interactions in rat islet β-cell secretion in vitro: Role of α6β1 integrin
    • Bosco, D., Meda, P., Halban, P. A., and Rouiller, D. G. (2000) Importance of cell-matrix interactions in rat islet β cell secretion in vitro. Role of α6β1 integrin. Diabetes 49, 233-243 (Pubitemid 30071002)
    • (2000) Diabetes , vol.49 , Issue.2 , pp. 233-243
    • Bosco, D.1    Meda, P.2    Halban, P.A.3    Rouiller, D.G.4
  • 30
    • 33745303353 scopus 로고    scopus 로고
    • Blockade of β1 integrin-laminin-5 interaction affects spreading and insulin secretion of rat β-cells attached on extracellular matrix
    • DOI 10.2337/db05-1388
    • Parnaud, G., Hammar, E., Rouiller, D. G., Armanet, M., Halban, P. A., and Bosco, D. (2006) Blockade of β1 integrin-laminin-5 interaction affects spreading and insulin secretion of rat β cells attached on extracellular matrix. Diabetes 55, 1413-1420 (Pubitemid 44195381)
    • (2006) Diabetes , vol.55 , Issue.5 , pp. 1413-1420
    • Parnaud, G.1    Hammar, E.2    Rouiller, D.G.3    Armanet, M.4    Halban, P.A.5    Bosco, D.6
  • 31
    • 70349150179 scopus 로고    scopus 로고
    • β1 integrin/FAK/ERK signaling pathway is essential for human fetal islet cell differentiation and survival
    • Saleem, S., Li, J., Yee, S. P., Fellows, G. F., Goodyer, C. G., and Wang, R. (2009) β1 integrin/FAK/ERK signaling pathway is essential for human fetal islet cell differentiation and survival. J. Pathol 219, 182-192
    • (2009) J. Pathol , vol.219 , pp. 182-192
    • Saleem, S.1    Li, J.2    Yee, S.P.3    Fellows, G.F.4    Goodyer, C.G.5    Wang, R.6
  • 32
    • 79951660073 scopus 로고    scopus 로고
    • Integrin α3, but not β1, regulates islet cell survival and function via PI3K/Akt signaling pathways
    • Krishnamurthy, M., Li, J., Fellows, G. F., Rosenberg, L., Goodyer, C. G., and Wang, R. (2011) Integrin α3, but not β1, regulates islet cell survival and function via PI3K/Akt signaling pathways. Endocrinology 152, 424-435
    • (2011) Endocrinology , vol.152 , pp. 424-435
    • Krishnamurthy, M.1    Li, J.2    Fellows, G.F.3    Rosenberg, L.4    Goodyer, C.G.5    Wang, R.6
  • 33
    • 0035399557 scopus 로고    scopus 로고
    • Lighting up the cell surface with evanescent wave microscopy
    • DOI 10.1016/S0962-8924(01)02027-X
    • Toomre, D., and Manstein, D. J. (2001) Lighting up the cell surface with evanescent wave microscopy. Trends Cell Biol. 11, 298-303 (Pubitemid 32537776)
    • (2001) Trends in Cell Biology , vol.11 , Issue.7 , pp. 298-303
    • Toomre, D.1    Manstein, D.J.2
  • 34
    • 0024150623 scopus 로고
    • Focal adhesions: Transmembrane junctions between the extracellular matrix and the cytoskeleton
    • Burridge, K., Fath, K., Kelly, T., Nuckolls, G., and Turner, C. (1988) Focal adhesions. Transmembrane junctions between the extracellular matrix and the cytoskeleton. Ann. Rev. Cell Biol. 4, 487-525 (Pubitemid 19139264)
    • (1988) Annual Review of Cell Biology , vol.4 , pp. 487-525
    • Burridge, K.1    Fath, K.2    Kelly, T.3    Nuckolls, G.4    Turner, C.5
  • 35
    • 0029257377 scopus 로고
    • Signal transduction through integrins. A central role for focal adhesion kinase?
    • Richardson, A., and Parsons, J. T. (1995) Signal transduction through integrins. A central role for focal adhesion kinase? Bioessays 17, 229-236
    • (1995) Bioessays , vol.17 , pp. 229-236
    • Richardson, A.1    Parsons, J.T.2
  • 36
    • 0033551899 scopus 로고    scopus 로고
    • Integrin signaling
    • Giancotti, F. G., and Ruoslahti, E. (1999) Integrin signaling. Science 285, 1028-1032
    • (1999) Science , vol.285 , pp. 1028-1032
    • Giancotti, F.G.1    Ruoslahti, E.2
  • 37
    • 0030585426 scopus 로고    scopus 로고
    • Molecular mechanisms for focal adhesion assembly through regulation of protein-protein interactions
    • Gilmore, A. P., and Burridge, K. (1996) Molecular mechanisms for focal adhesion assembly through regulation of protein-protein interactions. Structure 4, 647-651 (Pubitemid 126661286)
    • (1996) Structure , vol.4 , Issue.6 , pp. 647-651
    • Gilmore, A.P.1    Burridge, K.2
  • 38
    • 57349153946 scopus 로고    scopus 로고
    • A small molecule inhibitor, 1,2,4,5-benzenetetraamine tetrahydrochloride, targeting the Tyr-397 site of focal adhesion kinase decreases tumor growth
    • Golubovskaya, V. M., Nyberg, C., Zheng, M., Kweh, F., Magis, A., Ostrov, D., and Cance, W. G. (2008) A small molecule inhibitor, 1,2,4,5- benzenetetraamine tetrahydrochloride, targeting the Tyr-397 site of focal adhesion kinase decreases tumor growth. J. Med. Chem. 51, 7405-7416
    • (2008) J. Med. Chem. , vol.51 , pp. 7405-7416
    • Golubovskaya, V.M.1    Nyberg, C.2    Zheng, M.3    Kweh, F.4    Magis, A.5    Ostrov, D.6    Cance, W.G.7
  • 41
    • 52949150137 scopus 로고    scopus 로고
    • Focal adhesion kinase contributes to insulin-induced actin reorganization into a mesh harboring glucose transporter-4 in insulin-resistant skeletal muscle cells
    • Bisht, B., and Dey, C. S. (2008) Focal adhesion kinase contributes to insulin-induced actin reorganization into a mesh harboring glucose transporter-4 in insulin-resistant skeletal muscle cells. BMC Cell Biol. 9, 48
    • (2008) BMC Cell Biol. , vol.9 , pp. 48
    • Bisht, B.1    Dey, C.S.2
  • 42
    • 0015061581 scopus 로고
    • The stimulus-secretion coupling of glucose-induced insulin release. V. The participation of a microtubular-microfilamentous system
    • Malaisse, W. J., Malaisse-Lagae, F., Walker, M. O., and Lacy, P. E. (1971) The stimulus-secretion coupling of glucose-induced insulin release. V. The participation of a microtubular-microfilamentous system. Diabetes 20, 257-265
    • (1971) Diabetes , vol.20 , pp. 257-265
    • Malaisse, W.J.1    Malaisse-Lagae, F.2    Walker, M.O.3    Lacy, P.E.4
  • 43
    • 0346732321 scopus 로고    scopus 로고
    • 5′-AMP-activated Protein Kinase Controls Insulin-containing Secretory Vesicle Dynamics
    • DOI 10.1074/jbc.M307800200
    • Tsuboi, T., da Silva Xavier, G., Leclerc, I., and Rutter, G. A. (2003) 5′-AMP-activated protein kinase controls insulin-containing secretory vesicle dynamics. J. Biol. Chem. 278, 52042-52051 (Pubitemid 38035789)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.52 , pp. 52042-52051
    • Tsuboi, T.1    Da, S.X.G.2    Leclerc, I.3    Rutter, G.A.4
  • 44
    • 44849135266 scopus 로고    scopus 로고
    • Filamentous actin regulates insulin exocytosis through direct interaction with syntaxin 4
    • Jewell, J. L., Luo, W., Oh, E., Wang, Z., and Thurmond, D. C. (2008) Filamentous actin regulates insulin exocytosis through direct interaction with syntaxin 4. J. Biol. Chem. 283, 10716-10726
    • (2008) J. Biol. Chem. , vol.283 , pp. 10716-10726
    • Jewell, J.L.1    Luo, W.2    Oh, E.3    Wang, Z.4    Thurmond, D.C.5
  • 45
    • 0037380131 scopus 로고    scopus 로고
    • Multiple forms of "kiss-and-run" exocytosis revealed by evanescent wave microscopy
    • DOI 10.1016/S0960-9822(03)00176-3
    • Tsuboi, T., and Rutter, G. A. (2003) Multiple forms of "kiss-and-run"exocytosis revealed by evanescent wave microscopy. Curr. Biol. 13, 563-567 (Pubitemid 36391933)
    • (2003) Current Biology , vol.13 , Issue.7 , pp. 563-567
    • Tsuboi, T.1    Rutter, G.A.2
  • 46
    • 33744474156 scopus 로고    scopus 로고
    • Sustained exposure to high glucose concentrations modifies glucose signaling and the mechanics of secretory vesicle fusion in primary rat pancreatic β-cells
    • DOI 10.2337/diabetes.55.04.06.db05-1577
    • Tsuboi, T., Ravier, M. A., Parton, L. E., and Rutter, G. A. (2006) Sustained exposure to high glucose concentrations modifies glucose signaling and the mechanics of secretory vesicle fusion in primary rat pancreatic β cells. Diabetes 55, 1057-1065 (Pubitemid 44100182)
    • (2006) Diabetes , vol.55 , Issue.4 , pp. 1057-1065
    • Tsuboi, T.1    Ravier, M.A.2    Parton, L.E.3    Rutter, G.A.4
  • 47
    • 0842312945 scopus 로고    scopus 로고
    • Skeletal muscle cells and adipocytes differ in their reliance on TC10 and Rac for insulin-induced actin remodeling
    • JeBailey, L., Rudich, A., Huang, X., Di Ciano-Oliveira, C., Kapus, A., and Klip, A. (2004) Skeletal muscle cells and adipocytes differ in their reliance on TC10 and Rac for insulin-induced actin remodeling. Mol. Endocrinol. 18, 359-372
    • (2004) Mol. Endocrinol. , vol.18 , pp. 359-372
    • JeBailey, L.1    Rudich, A.2    Huang, X.3    Di Ciano-Oliveira, C.4    Kapus, A.5    Klip, A.6
  • 48
    • 0037677096 scopus 로고    scopus 로고
    • Insulin-stimulated phosphorylation of a Rab GTPase-activating protein regulates GLUT4 translocation
    • DOI 10.1074/jbc.C300063200
    • Sano, H., Kane, S., Sano, E., Mîinea, C. P., Asara, J. M., Lane, W. S., Garner, C. W., and Lienhard, G. E. (2003) Insulin-stimulated phosphorylation of a Rab GTPase-activating protein regulates GLUT4 translocation. J. Biol. Chem. 278, 14599-14602 (Pubitemid 36799780)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.17 , pp. 14599-14602
    • Sano, H.1    Kane, S.2    Sano, E.3    Miinea, C.P.4    Asara, J.M.5    Lane, W.S.6    Garner, C.W.7    Lienhard, G.E.8
  • 49
    • 33847062845 scopus 로고    scopus 로고
    • The Rab GTPase-activating protein AS160 integrates Akt, protein kinase C, and AMP-activated protein kinase signals regulating GLUT4 traffic
    • Thong, F. S., Bilan, P. J., and Klip, A. (2007) The Rab GTPase-activating protein AS160 integrates Akt, protein kinase C, and AMP-activated protein kinase signals regulating GLUT4 traffic. Diabetes 56, 414-423
    • (2007) Diabetes , vol.56 , pp. 414-423
    • Thong, F.S.1    Bilan, P.J.2    Klip, A.3
  • 50
    • 56649105132 scopus 로고    scopus 로고
    • Regulatory roles for Tiam1, a guanine nucleotide exchange factor for Rac1, in glucose-stimulated insulin secretion in pancreatic β cells
    • Veluthakal, R., Madathilparambil, S. V., McDonald, P., Olson, L. K., and Kowluru, A. (2009) Regulatory roles for Tiam1, a guanine nucleotide exchange factor for Rac1, in glucose-stimulated insulin secretion in pancreatic β cells. Biochem. Pharmacol. 77, 101-113
    • (2009) Biochem. Pharmacol. , vol.77 , pp. 101-113
    • Veluthakal, R.1    Madathilparambil, S.V.2    McDonald, P.3    Olson, L.K.4    Kowluru, A.5
  • 53
    • 77956460771 scopus 로고    scopus 로고
    • Polyamine-dependent activation of Rac1 is stimulated by focal adhesion-mediated Tiam1 activation
    • Elias, B. C., Bhattacharya, S., Ray, R. M., and Johnson, L. R. (2010) Polyamine-dependent activation of Rac1 is stimulated by focal adhesion-mediated Tiam1 activation. Cell Adh. Migr. 4, 419-430
    • (2010) Cell Adh. Migr. , vol.4 , pp. 419-430
    • Elias, B.C.1    Bhattacharya, S.2    Ray, R.M.3    Johnson, L.R.4
  • 54
    • 77649222989 scopus 로고    scopus 로고
    • Rac1 inactivation by lethal toxin from Clostridium sordellii modifies focal adhesions upstream of actin depolymerization
    • Geny, B., Grassart, A., Manich, M., Chicanne, G., Payrastre, B., Sauvonnet, N., and Popoff, M. R. (2010) Rac1 inactivation by lethal toxin from Clostridium sordellii modifies focal adhesions upstream of actin depolymerization. Cell. Microbiol. 12, 217-232
    • (2010) Cell. Microbiol. , vol.12 , pp. 217-232
    • Geny, B.1    Grassart, A.2    Manich, M.3    Chicanne, G.4    Payrastre, B.5    Sauvonnet, N.6    Popoff, M.R.7
  • 55
    • 48449102210 scopus 로고    scopus 로고
    • Rab GTPase-activating protein AS160 is a major downstream effector of protein kinase B/Akt signaling in pancreatic β cells
    • Bouzakri, K., Ribaux, P., Tomas, A., Parnaud, G., Rickenbach, K., and Halban, P. A. (2008) Rab GTPase-activating protein AS160 is a major downstream effector of protein kinase B/Akt signaling in pancreatic β cells. Diabetes 57, 1195-1204
    • (2008) Diabetes , vol.57 , pp. 1195-1204
    • Bouzakri, K.1    Ribaux, P.2    Tomas, A.3    Parnaud, G.4    Rickenbach, K.5    Halban, P.A.6
  • 56
    • 11144227239 scopus 로고    scopus 로고
    • 1
    • DOI 10.1074/jbc.M411202200
    • Kaido, T., Yebra, M., Cirulli, V., and Montgomery, A. M. (2004) Regulation of human β cell adhesion, motility, and insulin secretion by collagen IV and its receptor α1β1. J. Biol. Chem. 279, 53762-53769 (Pubitemid 40051885)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.51 , pp. 53762-53769
    • Kaido, T.1    Yebra, M.2    Cirulli, V.3    Montgomery, A.M.4
  • 58
    • 0026445719 scopus 로고
    • Tyrosine phosphorylation of paxillin and pp125FAK accompanies cell adhesion to extracellular matrix. A role in cytoskeletal assembly
    • Burridge, K., Turner, C. E., and Romer, L. H. (1992) Tyrosine phosphorylation of paxillin and pp125FAK accompanies cell adhesion to extracellular matrix. A role in cytoskeletal assembly. J. Cell Biol. 119, 893-903
    • (1992) J. Cell Biol. , vol.119 , pp. 893-903
    • Burridge, K.1    Turner, C.E.2    Romer, L.H.3
  • 59
    • 0026770377 scopus 로고
    • Integrins; versatility, modulation, and signaling in cell adhesion
    • Hynes, R. O. (1992) Integrins; versatility, modulation, and signaling in cell adhesion. Cell 69, 11-25
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 60
    • 0031574440 scopus 로고    scopus 로고
    • Identification and characterization of α3β1 integrin on primary and transformed rat islet cells
    • DOI 10.1006/excr.1997.3803
    • Kantengwa, S., Baetens, D., Sadoul, K., Buck, C. A., Halban, P. A., and Rouiller, D. G. (1997) Identification and characterization of α3β1 integrin on primary and transformed rat islet cells. Exp. Cell Res. 237, 394-402 (Pubitemid 28027934)
    • (1997) Experimental Cell Research , vol.237 , Issue.2 , pp. 394-402
    • Kantengwa, S.1    Baetens, D.2    Sadoul, K.3    Buck, C.A.4    Halban, P.A.5    Rouiller, D.G.6
  • 61
    • 3242786441 scopus 로고    scopus 로고
    • Extracellular matrix protects pancreatic β-cells against apoptosis: Role of short- and long-term signaling pathways
    • DOI 10.2337/diabetes.53.8.2034
    • Hammar, E., Parnaud, G., Bosco, D., Perriraz, N., Maedler, K., Donath, M., Rouiller, D. G., and Halban, P. A. (2004) Extracellular matrix protects pancreatic β cells against apoptosis. Role of short and long term signaling pathways. Diabetes 53, 2034-2041 (Pubitemid 38970752)
    • (2004) Diabetes , vol.53 , Issue.8 , pp. 2034-2041
    • Hammar, E.1    Parnaud, G.2    Bosco, D.3    Perriraz, N.4    Maedler, K.5    Donath, M.6    Rouiller, D.G.7    Halban, P.A.8
  • 62
    • 79953783426 scopus 로고    scopus 로고
    • Conditional β1-integrin-deficient mice display impaired pancreatic β cell function
    • Riopel, M., Krishnamurthy, M., Li, J., Liu, S., Leask, A., and Wang, R. (2011) Conditional β1-integrin-deficient mice display impaired pancreatic β cell function. J. Pathol. 224, 45-55
    • (2011) J. Pathol. , vol.224 , pp. 45-55
    • Riopel, M.1    Krishnamurthy, M.2    Li, J.3    Liu, S.4    Leask, A.5    Wang, R.6
  • 63
    • 0030005414 scopus 로고    scopus 로고
    • Actin disruption inhibits bombesin stimulation of focal adhesion kinase (pp125FAK) in prostate carcinoma
    • Duncan, M. D., Harmon, J. W., and Duncan, L. K. (1996) Actin disruption inhibits bombesin stimulation of focal adhesion kinase (pp125FAK) in prostate carcinoma. J. Surg. Res. 63, 359-363
    • (1996) J. Surg. Res. , vol.63 , pp. 359-363
    • Duncan, M.D.1    Harmon, J.W.2    Duncan, L.K.3
  • 64
    • 0035017538 scopus 로고    scopus 로고
    • Cas, and paxillin in Swiss 3T3 cells
    • DOI 10.1002/jcp.1102
    • Leopoldt, D., Yee, H. F., Jr., and Rozengurt, E. (2001) Calyculin A induces focal adhesion assembly and tyrosine phosphorylation of p125(Fak), p130(Cas), and paxillin in Swiss 3T3 cells. J. Cell. Physiol. 188, 106-119 (Pubitemid 32476501)
    • (2001) Journal of Cellular Physiology , vol.188 , Issue.1 , pp. 106-119
    • Leopoldt, D.1    Yee Jr., H.F.2    Rozengurt, E.3
  • 65
    • 0037088851 scopus 로고    scopus 로고
    • Modulatory role of focal adhesion kinase in regulating human pulmonary arterial endothelial barrier function
    • DOI 10.1113/jphysiol.2001.013289
    • Mehta, D., Tiruppathi, C., Sandoval, R., Minshall, R. D., Holinstat, M., and Malik, A. B. (2002) Modulatory role of focal adhesion kinase in regulating human pulmonary arterial endothelial barrier function. J. Physiol. 539, 779-789 (Pubitemid 35175429)
    • (2002) Journal of Physiology , vol.539 , Issue.3 , pp. 779-789
    • Mehta, D.1    Tiruppathi, C.2    Sandoval, R.3    Minshall, R.D.4    Holinstat, M.5    Malik, A.B.6
  • 66
    • 27144544079 scopus 로고    scopus 로고
    • The role of the cytoskeleton in differentially regulating pressure-mediated effects on malignant colonocyte focal adhesion signaling and cell adhesion
    • DOI 10.1093/carcin/bgi135
    • Thamilselvan, V., and Basson, M. D. (2005) The role of the cytoskeleton in differentially regulating pressure-mediated effects on malignant colonocyte focal adhesion signaling and cell adhesion. Carcinogenesis 26, 1687-1697 (Pubitemid 41487984)
    • (2005) Carcinogenesis , vol.26 , Issue.10 , pp. 1687-1697
    • Thamilselvan, V.1    Basson, M.D.2
  • 67
    • 66849115296 scopus 로고    scopus 로고
    • Mechanisms of biphasic insulin-granule exocytosis. Roles of the cytoskeleton, small GTPases, and SNARE proteins
    • Wang, Z., and Thurmond, D. C. (2009) Mechanisms of biphasic insulin-granule exocytosis. Roles of the cytoskeleton, small GTPases, and SNARE proteins. J. Cell Sci. 122, 893-903
    • (2009) J. Cell Sci. , vol.122 , pp. 893-903
    • Wang, Z.1    Thurmond, D.C.2
  • 70
    • 1542319211 scopus 로고    scopus 로고
    • Site of Docking and Fusion of Insulin Secretory Granules in Live MIN6 β Cells Analyzed by TAT-conjugated Anti-syntaxin 1 Antibody and Total Internal Reflection Fluorescence Microscopy
    • DOI 10.1074/jbc.M308954200
    • Ohara-Imaizumi, M., Nishiwaki, C., Kikuta, T., Kumakura, K., Nakamichi, Y., and Nagamatsu, S. (2004) Site of docking and fusion of insulin secretory granules in live MIN6β cells analyzed by TAT-conjugated anti-syntaxin 1 antibody and total internal reflection fluorescence microscopy. J. Biol. Chem. 279, 8403-8408 (Pubitemid 38294733)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.9 , pp. 8403-8408
    • Ohara-Imaizumi, M.1    Nishiwaki, C.2    Kikuta, T.3    Kumakura, K.4    Nakamichi, Y.5    Nagamatsu, S.6
  • 71
    • 0029760302 scopus 로고    scopus 로고
    • 2+ channels
    • Wiser, O., Bennett, M. K., and Atlas, D. (1996) Functional interaction of syntaxin and SNAP-25 with voltage-sensitive L- and N-type Ca2+ channels. EMBO J. 15, 4100-4110 (Pubitemid 26278693)
    • (1996) EMBO Journal , vol.15 , Issue.16 , pp. 4100-4110
    • Wiser, O.1    Bennett, M.K.2    Atlas, D.3
  • 74
    • 0030721973 scopus 로고    scopus 로고
    • Evidence for differential roles of the Rho subfamily of GTP-binding proteins in glucose- and calcium-induced insulin secretion from pancreatic β cells
    • DOI 10.1016/S0006-2952(97)00314-6, PII S0006295297003146
    • Kowluru, A., Li, G., Rabaglia, M. E., Segu, V. B., Hofmann, F., Aktories, K., and Metz, S. A. (1997) Evidence for differential roles of the Rho subfamily of GTP-binding proteins in glucose- and calcium-induced insulin secretion from pancreatic β cells. Biochem. Pharmacol. 54, 1097-1108 (Pubitemid 27479023)
    • (1997) Biochemical Pharmacology , vol.54 , Issue.10 , pp. 1097-1108
    • Kowluru, A.1    Li, G.2    Rabaglia, M.E.3    Segu, V.B.4    Hofmann, F.5    Aktories, K.6    Metz, S.A.7
  • 75
    • 0141646523 scopus 로고    scopus 로고
    • Novel roles for the Rho subfamily of GTP-binding proteins in succinate-induced insulin secretion from βTC3 cells: Further evidence in support of the succinate mechanism of insulin release
    • DOI 10.1081/ERC-120025043
    • Kowluru, A., Chen, H. Q., and Tannous, M. (2003) Novel roles for the Rho subfamily of GTP-binding proteins in succinate-induced insulin secretion from βTC3 cells. Further evidence in support of the succinate mechanism of insulin release. Endocr. Res. 29, 363-376 (Pubitemid 37176595)
    • (2003) Endocrine Research , vol.29 , Issue.3 , pp. 363-376
    • Kowluru, A.1    Chen, H.-Q.2    Tannous, M.3
  • 76
    • 0141450545 scopus 로고    scopus 로고
    • Mastoparan-induced insulin secretion from insulin-secreting βTC3 and INS-1 cells: Evidence for its regulation by rho subfamily of G proteins
    • DOI 10.1210/en.2003-0106
    • Amin, R. H., Chen, H. Q., Veluthakal, R., Silver, R. B., Li, J., Li, G., and Kowluru, A. (2003) Mastoparan-induced insulin secretion from insulin-secreting βTC3 and INS-1 cells. Evidence for its regulation by Rho subfamily of G proteins. Endocrinology 144, 4508-4518 (Pubitemid 37204850)
    • (2003) Endocrinology , vol.144 , Issue.10 , pp. 4508-4518
    • Amin, R.H.1    Chen, H.-Q.2    Veluthakal, R.3    Silver, R.B.4    Li, J.5    Li, G.6    Kowluru, A.7
  • 77
    • 1942472545 scopus 로고    scopus 로고
    • Novel regulation by Rac1 of glucose- and forskolin-induced insulin secretion in INS-1 β-cells
    • DOI 10.1152/ajpendo.00307.2003
    • Li, J., Luo, R., Kowluru, A., and Li, G. (2004) Novel regulation by Rac1 of glucose- and forskolin-induced insulin secretion in INS-1 β cells. Am. J. Physiol. Endocrinol. Metab. 286, E818-E827 (Pubitemid 38514676)
    • (2004) American Journal of Physiology - Endocrinology and Metabolism , vol.286 , Issue.5
    • Li, J.1    Luo, R.2    Kowluru, A.3    Li, G.4
  • 78
    • 55249098126 scopus 로고    scopus 로고
    • GLUT4 vesicle recruitment and fusion are differentially regulated by Rac, AS160, and Rab8A in muscle cells
    • Randhawa, V. K., Ishikura, S., Talior-Volodarsky, I., Cheng, A. W., Patel, N., Hartwig, J. H., and Klip, A. (2008) GLUT4 vesicle recruitment and fusion are differentially regulated by Rac, AS160, and Rab8A in muscle cells. J. Biol. Chem. 283, 27208-27219
    • (2008) J. Biol. Chem. , vol.283 , pp. 27208-27219
    • Randhawa, V.K.1    Ishikura, S.2    Talior-Volodarsky, I.3    Cheng, A.W.4    Patel, N.5    Hartwig, J.H.6    Klip, A.7
  • 79
    • 66349098674 scopus 로고    scopus 로고
    • Insulin-modulated Akt subcellular localization determines Akt isoform-specific signaling
    • Gonzalez, E., and McGraw, T. E. (2009) Insulin-modulated Akt subcellular localization determines Akt isoform-specific signaling. Proc. Natl. Acad. Sci. U.S.A. 106, 7004-7009
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 7004-7009
    • Gonzalez, E.1    McGraw, T.E.2
  • 80
    • 33847026801 scopus 로고    scopus 로고
    • Ceramide- and oxidant-induced insulin resistance involve loss of insulin-dependent Rac-activation and actin remodeling in muscle cells
    • JeBailey, L., Wanono, O., Niu, W., Roessler, J., Rudich, A., and Klip, A. (2007) Ceramide- and oxidant-induced insulin resistance involve loss of insulin-dependent Rac-activation and actin remodeling in muscle cells. Diabetes 56, 394-403
    • (2007) Diabetes , vol.56 , pp. 394-403
    • JeBailey, L.1    Wanono, O.2    Niu, W.3    Roessler, J.4    Rudich, A.5    Klip, A.6
  • 81
    • 37249087851 scopus 로고    scopus 로고
    • Small G proteins in insulin action: Rab and Rho families at the crossroads of signal transduction and GLUT4 vesicle traffic
    • DOI 10.1111/j.1748-1716.2007.01778.x
    • Ishikura, S., Koshkina, A., and Klip, A. (2008) Small G proteins in insulin action. Rab and Rho families at the crossroads of signal transduction and GLUT4 vesicle traffic. Acta physiol. (Oxf) 192, 61-74 (Pubitemid 350265359)
    • (2008) Acta Physiologica , vol.192 , Issue.1 , pp. 61-74
    • Ishikura, S.1    Koshkina, A.2    Klip, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.