메뉴 건너뛰기




Volumn 6, Issue , 2015, Pages

Tropomodulin3 is a novel Akt2 effector regulating insulin-stimulated GLUT4 exocytosis through cortical actin remodeling

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN BINDING PROTEIN; ACTIN CAPPING PROTEIN; F ACTIN; G ACTIN; GLUCOSE TRANSPORTER 4; LATRUNCULIN B; PROTEIN KINASE B BETA; TROPOMODULIN; TROPOMODULIN 3; UNCLASSIFIED DRUG; ACTIN; AKT2 PROTEIN, HUMAN; AKT2 PROTEIN, MOUSE; GLUCOSE; INSULIN; PROTEIN KINASE B; SLC2A4 PROTEIN, HUMAN; SLC2A4 PROTEIN, MOUSE; TMOD3 PROTEIN, HUMAN; TMOD3 PROTEIN, MOUSE;

EID: 84986571401     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms6951     Document Type: Article
Times cited : (71)

References (70)
  • 1
    • 84861890085 scopus 로고    scopus 로고
    • Regulation of glucose transporter translocation in health and diabetes
    • Bogan, J. S. Regulation of glucose transporter translocation in health and diabetes. Annu. Rev. Biochem. 81, 507-532 (2012).
    • (2012) Annu. Rev. Biochem. , vol.81 , pp. 507-532
    • Bogan, J.S.1
  • 3
    • 33947596679 scopus 로고    scopus 로고
    • The GLUT4 glucose transporter
    • Huang, S. & Czech, M. P. The GLUT4 glucose transporter. Cell Metab. 5, 237-252 (2007).
    • (2007) Cell Metab. , vol.5 , pp. 237-252
    • Huang, S.1    Czech, M.P.2
  • 5
    • 84861444859 scopus 로고    scopus 로고
    • Regulation of glucose transport by insulin: Traffic control of GLUT4
    • Leto, D. & Saltiel, A. R. Regulation of glucose transport by insulin: traffic control of GLUT4. Nat. Rev. Mol. Cell Biol. 13, 383-396 (2012).
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 383-396
    • Leto, D.1    Saltiel, A.R.2
  • 6
    • 79953841907 scopus 로고    scopus 로고
    • Endocytosis, recycling, and regulated exocytosis of glucose transporter 4
    • Foley, K., Boguslavsky, S. & Klip, A. Endocytosis, recycling, and regulated exocytosis of glucose transporter 4. Biochemistry 50, 3048-3061 (2011).
    • (2011) Biochemistry , vol.50 , pp. 3048-3061
    • Foley, K.1    Boguslavsky, S.2    Klip, A.3
  • 7
    • 79952107840 scopus 로고    scopus 로고
    • Signaling, cytoskeletal and membrane mechanisms regulating GLUT4 exocytosis
    • Hoffman, N. J. & Elmendorf, J. S. Signaling, cytoskeletal and membrane mechanisms regulating GLUT4 exocytosis. Trends Endocrinol. Metab. 22, 110-116 (2011).
    • (2011) Trends Endocrinol. Metab. , vol.22 , pp. 110-116
    • Hoffman, N.J.1    Elmendorf, J.S.2
  • 8
    • 1542781732 scopus 로고    scopus 로고
    • Isoform-specific regulation of insulin-dependent glucose uptake by Akt/protein kinase B
    • Bae, S. S., Cho, H., Mu, J. & Birnbaum, M. J. Isoform-specific regulation of insulin-dependent glucose uptake by Akt/protein kinase B. J. Biol. Chem. 278, 49530-49536 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 49530-49536
    • Bae, S.S.1    Cho, H.2    Mu, J.3    Birnbaum, M.J.4
  • 9
    • 2542528670 scopus 로고    scopus 로고
    • A family with severe insulin resistance and diabetes due to a mutation in AKT2
    • George, S. et al. A family with severe insulin resistance and diabetes due to a mutation in AKT2. Science 304, 1325-1328 (2004).
    • (2004) Science , vol.304 , pp. 1325-1328
    • George, S.1
  • 10
    • 0035368548 scopus 로고    scopus 로고
    • Insulin resistance and a diabetes mellitus-like syndrome in mice lacking the protein kinase Akt2 (PKB beta)
    • Cho, H. et al. Insulin resistance and a diabetes mellitus-like syndrome in mice lacking the protein kinase Akt2 (PKB beta). Science 292, 1728-1731 (2001).
    • (2001) Science , vol.292 , pp. 1728-1731
    • Cho, H.1
  • 11
    • 85047693348 scopus 로고    scopus 로고
    • Severe diabetes, age-dependent loss of adipose tissue, and mild growth deficiency in mice lacking Akt2/PKB beta
    • Garofalo, R. S. et al. Severe diabetes, age-dependent loss of adipose tissue, and mild growth deficiency in mice lacking Akt2/PKB beta. J. Clin. Invest. 112, 197-208 (2003).
    • (2003) J. Clin. Invest. , vol.112 , pp. 197-208
    • Garofalo, R.S.1
  • 12
    • 34548436875 scopus 로고    scopus 로고
    • GLUT4 translocation: The last 200 nanometers
    • Watson, R. T. & Pessin, J. E. GLUT4 translocation: the last 200 nanometers. Cell. Signal. 19, 2209-2217 (2007).
    • (2007) Cell. Signal. , vol.19 , pp. 2209-2217
    • Watson, R.T.1    Pessin, J.E.2
  • 13
    • 0037677096 scopus 로고    scopus 로고
    • Insulin-stimulated phosphorylation of a Rab GTPase-activating protein regulates GLUT4 translocation
    • Sano, H. et al. Insulin-stimulated phosphorylation of a Rab GTPase-activating protein regulates GLUT4 translocation. J. Biol. Chem. 278, 14599-14602 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 14599-14602
    • Sano, H.1
  • 14
    • 79960665062 scopus 로고    scopus 로고
    • Loss of AS160 Akt substrate causes Glut4 protein to accumulate in compartments that are primed for fusion in basal adipocytes
    • Brewer, P. D., Romenskaia, I., Kanow, M. A. & Mastick, C. C. Loss of AS160 Akt substrate causes Glut4 protein to accumulate in compartments that are primed for fusion in basal adipocytes. J. Biol. Chem. 286, 26287-26297 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 26287-26297
    • Brewer, P.D.1    Romenskaia, I.2    Kanow, M.A.3    Mastick, C.C.4
  • 15
    • 80052770295 scopus 로고    scopus 로고
    • C2 domain-containing phosphoprotein CDP138 regulates GLUT4 insertion into the plasma membrane
    • Xie, X. et al. C2 domain-containing phosphoprotein CDP138 regulates GLUT4 insertion into the plasma membrane. Cell Metab. 14, 378-389 (2011).
    • (2011) Cell Metab. , vol.14 , pp. 378-389
    • Xie, X.1
  • 16
    • 33845666593 scopus 로고    scopus 로고
    • Dissecting multiple steps of GLUT4 trafficking and identifying the sites of insulin action
    • Bai, L. et al. Dissecting multiple steps of GLUT4 trafficking and identifying the sites of insulin action. Cell Metab. 5, 47-57 (2007).
    • (2007) Cell Metab. , vol.5 , pp. 47-57
    • Bai, L.1
  • 17
    • 27744584659 scopus 로고    scopus 로고
    • Insulin signaling meets vesicle traffic of GLUT4 at a plasma-membrane-activated fusion step
    • Koumanov, F., Jin, B., Yang, J. & Holman, G. D. Insulin signaling meets vesicle traffic of GLUT4 at a plasma-membrane-activated fusion step. Cell Metab. 2, 179-189 (2005).
    • (2005) Cell Metab. , vol.2 , pp. 179-189
    • Koumanov, F.1    Jin, B.2    Yang, J.3    Holman, G.D.4
  • 18
    • 34249052338 scopus 로고    scopus 로고
    • 'Actin'g on GLUT4: Membrane & cytoskeletal components of insulin action
    • Brozinick, J. T., Berkemeier, B. A. & Elmendorf, J. S. 'Actin'g on GLUT4: membrane & cytoskeletal components of insulin action. Curr. Diabetes Rev. 3, 111-122 (2007).
    • (2007) Curr. Diabetes Rev. , vol.3 , pp. 111-122
    • Brozinick, J.T.1    Berkemeier, B.A.2    Elmendorf, J.S.3
  • 19
    • 0034907579 scopus 로고    scopus 로고
    • Insulin-induced cortical actin remodeling promotes GLUT4 insertion at muscle cell membrane ruffles
    • Tong, P. et al. Insulin-induced cortical actin remodeling promotes GLUT4 insertion at muscle cell membrane ruffles. J. Clin. Invest. 108, 371-381 (2001).
    • (2001) J. Clin. Invest. , vol.108 , pp. 371-381
    • Tong, P.1
  • 20
    • 0028126854 scopus 로고
    • Disassembly of the actin network inhibits insulin-dependent stimulation of glucose transport and prevents recruitment of glucose transporters to the plasma membrane
    • Tsakiridis, T., Vranic, M. & Klip, A. Disassembly of the actin network inhibits insulin-dependent stimulation of glucose transport and prevents recruitment of glucose transporters to the plasma membrane. J. Biol. Chem. 269, 29934-29942 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 29934-29942
    • Tsakiridis, T.1    Vranic, M.2    Klip, A.3
  • 21
    • 0032080114 scopus 로고    scopus 로고
    • Actin filaments participate in the relocalization of phosphatidylinositol3-kinase to glucose transporter-containing compartments and in the stimulation of glucose uptake in 3T3-L1 adipocytes
    • Wang, Q., Bilan, P. J., Tsakiridis, T., Hinek, A. & Klip, A. Actin filaments participate in the relocalization of phosphatidylinositol3-kinase to glucose transporter-containing compartments and in the stimulation of glucose uptake in 3T3-L1 adipocytes. Biochem. J. 331, 917-928 (1998).
    • (1998) Biochem. J. , vol.331 , pp. 917-928
    • Wang, Q.1    Bilan, P.J.2    Tsakiridis, T.3    Hinek, A.4    Klip, A.5
  • 22
    • 70349307380 scopus 로고    scopus 로고
    • Identification of a distal GLUT4 trafficking event controlled by actin polymerization
    • Lopez, J. A. et al. Identification of a distal GLUT4 trafficking event controlled by actin polymerization. Mol. Biol. Cell 20, 3918-3929 (2009).
    • (2009) Mol. Biol. Cell , vol.20 , pp. 3918-3929
    • Lopez, J.A.1
  • 23
    • 84867444426 scopus 로고    scopus 로고
    • Myo1c binding to submembrane actin mediates insulininduced tethering of GLUT4 vesicles
    • Boguslavsky, S. et al. Myo1c binding to submembrane actin mediates insulininduced tethering of GLUT4 vesicles. Mol. Biol. Cell 23, 4065-4078 (2012).
    • (2012) Mol. Biol. Cell , vol.23 , pp. 4065-4078
    • Boguslavsky, S.1
  • 24
    • 0037180775 scopus 로고    scopus 로고
    • Glucose transporter recycling in response to insulin is facilitated by myosin Myo1c
    • Bose, A. et al. Glucose transporter recycling in response to insulin is facilitated by myosin Myo1c. Nature 420, 821-824 (2002).
    • (2002) Nature , vol.420 , pp. 821-824
    • Bose, A.1
  • 25
    • 54849439728 scopus 로고    scopus 로고
    • CaMKII-mediated phosphorylation of the myosin motor Myo1c is required for insulin-stimulated GLUT4 translocation in adipocytes
    • Yip, M. F. et al. CaMKII-mediated phosphorylation of the myosin motor Myo1c is required for insulin-stimulated GLUT4 translocation in adipocytes. Cell Metab. 8, 384-398 (2008).
    • (2008) Cell Metab. , vol.8 , pp. 384-398
    • Yip, M.F.1
  • 26
    • 33745613778 scopus 로고    scopus 로고
    • Insulin receptor signals regulating GLUT4 translocation and actin dynamics
    • Kanzaki, M. Insulin receptor signals regulating GLUT4 translocation and actin dynamics. Endocr. J. 53, 267-293 (2006).
    • (2006) Endocr. J. , vol.53 , pp. 267-293
    • Kanzaki, M.1
  • 27
    • 0035834644 scopus 로고    scopus 로고
    • Insulin-stimulated GLUT4 translocation in adipocytes is dependent upon cortical actin remodeling
    • Kanzaki, M. & Pessin, J. E. Insulin-stimulated GLUT4 translocation in adipocytes is dependent upon cortical actin remodeling. J. Biol. Chem. 276, 42436-42444 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 42436-42444
    • Kanzaki, M.1    Pessin, J.E.2
  • 28
    • 41449087811 scopus 로고    scopus 로고
    • Rapid activation of Akt2 is sufficient to stimulate GLUT4 translocation in 3T3-L1 adipocytes
    • Ng, Y., Ramm, G., Lopez, J. A. & James, D. E. Rapid activation of Akt2 is sufficient to stimulate GLUT4 translocation in 3T3-L1 adipocytes. Cell Metab. 7, 348-356 (2008).
    • (2008) Cell Metab. , vol.7 , pp. 348-356
    • Ng, Y.1    Ramm, G.2    Lopez, J.A.3    James, D.E.4
  • 29
    • 0029908016 scopus 로고    scopus 로고
    • Expression of a constitutively active Akt Ser/Thr kinase in 3T3-L1 adipocytes stimulates glucose uptake and glucose transporter 4 translocation
    • Kohn, A. D., Summers, S. A., Birnbaum, M. J. & Roth, R. A. Expression of a constitutively active Akt Ser/Thr kinase in 3T3-L1 adipocytes stimulates glucose uptake and glucose transporter 4 translocation. J. Biol. Chem. 271, 31372-31378 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 31372-31378
    • Kohn, A.D.1    Summers, S.A.2    Birnbaum, M.J.3    Roth, R.A.4
  • 30
    • 85027946629 scopus 로고    scopus 로고
    • Tropomodulins: Pointed-end capping proteins that regulate actin filament architecture in diverse cell types
    • Yamashiro, S., Gokhin, D. S., Kimura, S., Nowak, R. B. & Fowler, V. M. Tropomodulins: Pointed-end capping proteins that regulate actin filament architecture in diverse cell types. Cytoskeleton 69, 337-370 (2012).
    • (2012) Cytoskeleton , vol.69 , pp. 337-370
    • Yamashiro, S.1    Gokhin, D.S.2    Kimura, S.3    Nowak, R.B.4    Fowler, V.M.5
  • 31
    • 0034001356 scopus 로고    scopus 로고
    • Sequencing, expression analysis, and mapping of three unique human tropomodulin genes and their mouse orthologs
    • Cox, P. R. & Zoghbi, H. Y. Sequencing, expression analysis, and mapping of three unique human tropomodulin genes and their mouse orthologs. Genomics 63, 97-107 (2000).
    • (2000) Genomics , vol.63 , pp. 97-107
    • Cox, P.R.1    Zoghbi, H.Y.2
  • 32
    • 0038070120 scopus 로고    scopus 로고
    • Pointed-end capping by tropomodulin3 negatively regulates endothelial cell motility
    • Fischer, R. S., Fritz-Six, K. L. & Fowler, V. M. Pointed-end capping by tropomodulin3 negatively regulates endothelial cell motility. J. Cell Biol. 161, 371-380 (2003).
    • (2003) J. Cell Biol. , vol.161 , pp. 371-380
    • Fischer, R.S.1    Fritz-Six, K.L.2    Fowler, V.M.3
  • 33
    • 73349135982 scopus 로고    scopus 로고
    • The measurement of GLUT4 translocation in 3T3-L1 adipocytes
    • Konstantopoulos, N. & Molero-Navajas, J. C. The measurement of GLUT4 translocation in 3T3-L1 adipocytes. Methods Mol. Biol. 560, 111-135 (2009).
    • (2009) Methods Mol. Biol. , vol.560 , pp. 111-135
    • Konstantopoulos, N.1    Molero-Navajas, J.C.2
  • 34
    • 0035929258 scopus 로고    scopus 로고
    • Insulin-regulated trafficking of dual-labeled glucose transporter 4 in primary rat adipose cells
    • Dawson, K. Insulin-regulated trafficking of dual-labeled glucose transporter 4 in primary rat adipose cells. Biochem. Biophys. Res. Commun. 287, 445-454 (2001).
    • (2001) Biochem. Biophys. Res. Commun. , vol.287 , pp. 445-454
    • Dawson, K.1
  • 35
    • 77957747467 scopus 로고    scopus 로고
    • Mammalian tropomodulins nucleate actin polymerization via their actin monomer binding and filament pointed end-capping activities
    • Yamashiro, S., Speicher, K. D., Speicher, D. W. & Fowler, V. M. Mammalian tropomodulins nucleate actin polymerization via their actin monomer binding and filament pointed end-capping activities. J. Biol. Chem. 285, 33265-33280 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 33265-33280
    • Yamashiro, S.1    Speicher, K.D.2    Speicher, D.W.3    Fowler, V.M.4
  • 36
    • 46249118002 scopus 로고    scopus 로고
    • Lifeact: A versatile marker to visualize F-actin
    • Riedl, J. et al. Lifeact: a versatile marker to visualize F-actin. Nat. Methods 5, 605-607 (2008).
    • (2008) Nat. Methods , vol.5 , pp. 605-607
    • Riedl, J.1
  • 37
    • 33845967136 scopus 로고    scopus 로고
    • Tropomodulin 3 binds to actin monomers
    • Fischer, R. S. et al. Tropomodulin 3 binds to actin monomers. J. Biol. Chem. 281, 36454-36465 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 36454-36465
    • Fischer, R.S.1
  • 38
    • 77950579849 scopus 로고    scopus 로고
    • Tropomodulin isoforms regulate thin filament pointed-end capping and skeletal muscle physiology
    • Gokhin, D. S. et al. Tropomodulin isoforms regulate thin filament pointed-end capping and skeletal muscle physiology. J. Cell Biol. 189, 95-109 (2010).
    • (2010) J. Cell Biol. , vol.189 , pp. 95-109
    • Gokhin, D.S.1
  • 39
    • 0036841312 scopus 로고    scopus 로고
    • Crystal structure of the C-terminal half of tropomodulin and structural basis of actin filament pointed-end capping
    • Krieger, I., Kostyukova, A., Yamashita, A., Nitanai, Y. & Maéda, Y. Crystal structure of the C-terminal half of tropomodulin and structural basis of actin filament pointed-end capping. Biophys. J. 83, 2716-2725 (2002).
    • (2002) Biophys. J. , vol.83 , pp. 2716-2725
    • Krieger, I.1    Kostyukova, A.2    Yamashita, A.3    Nitanai, Y.4    Maéda, Y.5
  • 40
    • 78751507345 scopus 로고    scopus 로고
    • Identification of residues within tropomodulin-1 responsible for its localization at the pointed ends of the actin filaments in cardiac myocytes
    • Tsukada, T. et al. Identification of residues within tropomodulin-1 responsible for its localization at the pointed ends of the actin filaments in cardiac myocytes. J. Biol. Chem. 286, 2194-2204 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 2194-2204
    • Tsukada, T.1
  • 41
    • 33751076023 scopus 로고    scopus 로고
    • Loss of cortical actin filaments in insulin-resistant skeletal muscle cells impairs GLUT4 vesicle trafficking and glucose transport
    • McCarthy, A. M., Spisak, K. O., Brozinick, J. T. & Elmendorf, J. S. Loss of cortical actin filaments in insulin-resistant skeletal muscle cells impairs GLUT4 vesicle trafficking and glucose transport. Am. J. Physiol. Cell Physiol. 291, C860-C868 (2006).
    • (2006) Am. J. Physiol. Cell Physiol. , vol.291 , pp. C860-C868
    • McCarthy, A.M.1    Spisak, K.O.2    Brozinick, J.T.3    Elmendorf, J.S.4
  • 42
    • 0033962410 scopus 로고    scopus 로고
    • Insulin-induced actin filament remodeling colocalizes actin with phosphatidylinositol 3-kinase and GLUT4 in L6 myotubes
    • Khayat, Z. A., Tong, P., Yaworsky, K., Bloch, R. J. & Klip, A. Insulin-induced actin filament remodeling colocalizes actin with phosphatidylinositol 3-kinase and GLUT4 in L6 myotubes. J. Cell Sci. 113, 279-290 (2000).
    • (2000) J. Cell Sci. , vol.113 , pp. 279-290
    • Khayat, Z.A.1    Tong, P.2    Yaworsky, K.3    Bloch, R.J.4    Klip, A.5
  • 43
    • 84856715266 scopus 로고    scopus 로고
    • Fat-induced membrane cholesterol accrual provokes cortical filamentous actin destabilisation and glucose transport dysfunction in skeletal muscle
    • Habegger, K. M. et al. Fat-induced membrane cholesterol accrual provokes cortical filamentous actin destabilisation and glucose transport dysfunction in skeletal muscle. Diabetologia 55, 457-467 (2012).
    • (2012) Diabetologia , vol.55 , pp. 457-467
    • Habegger, K.M.1
  • 44
    • 0037016725 scopus 로고    scopus 로고
    • A phosphatidylinositol 3-kinase-independent insulin signaling pathway to N-WASP/Arp2/3/F-actin required for GLUT4 glucose transporter recycling
    • Jiang, Z. Y., Chawla, A., Bose, A., Way, M. & Czech, M. P. A phosphatidylinositol 3-kinase-independent insulin signaling pathway to N-WASP/Arp2/3/F-actin required for GLUT4 glucose transporter recycling. J. Biol. Chem. 277, 509-515 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 509-515
    • Jiang, Z.Y.1    Chawla, A.2    Bose, A.3    Way, M.4    Czech, M.P.5
  • 45
    • 2942534876 scopus 로고    scopus 로고
    • Unconventional myosin Myo1c promotes membrane fusion in a regulated exocytic pathway
    • Bose, A. et al. Unconventional myosin Myo1c promotes membrane fusion in a regulated exocytic pathway. Mol. Cell. Biol. 24, 5447-5458 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 5447-5458
    • Bose, A.1
  • 46
    • 77958063756 scopus 로고    scopus 로고
    • Arp2/3- and cofilin-coordinated actin dynamics is required for insulin-mediated GLUT4 translocation to the surface of muscle cells
    • Chiu, T. T., Patel, N., Shaw, A. E., Bamburg, J. R. & Klip, A. Arp2/3- and cofilin-coordinated actin dynamics is required for insulin-mediated GLUT4 translocation to the surface of muscle cells. Mol. Biol. Cell 21, 3529-3539 (2010).
    • (2010) Mol. Biol. Cell , vol.21 , pp. 3529-3539
    • Chiu, T.T.1    Patel, N.2    Shaw, A.E.3    Bamburg, J.R.4    Klip, A.5
  • 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. et al. Skeletal muscle cells and adipocytes differ in their reliance on TC10 and Rac for insulin-induced actin remodeling. Mol. Endocrinol. 18, 359-372 (2004).
    • (2004) Mol. Endocrinol. , vol.18 , pp. 359-372
    • JeBailey, L.1
  • 48
    • 77954447111 scopus 로고    scopus 로고
    • Crucial role of the small GTPase Rac1 in insulin-stimulated translocation of glucose transporter 4 to the mouse skeletal muscle sarcolemma
    • Ueda, S. et al. Crucial role of the small GTPase Rac1 in insulin-stimulated translocation of glucose transporter 4 to the mouse skeletal muscle sarcolemma. FASEB J. 24, 2254-2261 (2010).
    • (2010) FASEB J. , vol.24 , pp. 2254-2261
    • Ueda, S.1
  • 49
    • 4644260677 scopus 로고    scopus 로고
    • Disruption of cortical actin in skeletal muscle demonstrates an essential role of the cytoskeleton in glucose transporter 4 translocation in insulin-sensitive tissues
    • Brozinick, J. T., Hawkins, E. D., Strawbridge, A. B. & Elmendorf, J. S. Disruption of cortical actin in skeletal muscle demonstrates an essential role of the cytoskeleton in glucose transporter 4 translocation in insulin-sensitive tissues. J. Biol. Chem. 279, 40699-40706 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 40699-40706
    • Brozinick, J.T.1    Hawkins, E.D.2    Strawbridge, A.B.3    Elmendorf, J.S.4
  • 50
    • 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. et al. Ceramide- and oxidant-induced insulin resistance involve loss of insulin-dependent Rac-activation and actin remodeling in muscle cells. Diabetes 56, 394-403 (2007).
    • (2007) Diabetes , vol.56 , pp. 394-403
    • JeBailey, L.1
  • 51
    • 0029410624 scopus 로고
    • The GTP-binding protein Rac does not couple PI 3-kinase to insulin-stimulated glucose transport in adipocytes
    • Marcusohn, J., Isakoff, S. J., Rose, E., Symons, M. & Skolnik, E. Y. The GTP-binding protein Rac does not couple PI 3-kinase to insulin-stimulated glucose transport in adipocytes. Curr. Biol. 5, 1296-1302 (1995).
    • (1995) Curr. Biol. , vol.5 , pp. 1296-1302
    • Marcusohn, J.1    Isakoff, S.J.2    Rose, E.3    Symons, M.4    Skolnik, E.Y.5
  • 52
    • 0030707535 scopus 로고    scopus 로고
    • Changes in the signalling status of the small GTP-binding proteins Rac and Rho do not influence insulin-stimulated hexose transport
    • Dorrestijn, J., Bos, J. L., Van Der Zon, G. C. M. & Maassen, J. A. Changes in the signalling status of the small GTP-binding proteins Rac and Rho do not influence insulin-stimulated hexose transport. Exp. Clin. Endocrinol. Diabetes 105, 254-262 (1997).
    • (1997) Exp. Clin. Endocrinol. Diabetes , vol.105 , pp. 254-262
    • Dorrestijn, J.1    Bos, J.L.2    Van Der Zon, G.C.M.3    Maassen, J.A.4
  • 53
    • 0033049422 scopus 로고    scopus 로고
    • Protein kinase B/Akt participates in GLUT4 translocation by insulin in L6 myoblasts
    • Wang, Q. et al. Protein kinase B/Akt participates in GLUT4 translocation by insulin in L6 myoblasts. Mol. Cell. Biol. 19, 4008-4018 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4008-4018
    • Wang, Q.1
  • 54
    • 84876334507 scopus 로고    scopus 로고
    • Akt2 regulates Rac1 activity in the insulin-dependent signaling pathway leading to GLUT4 translocation to the plasma membrane in skeletal muscle cells
    • Nozaki, S. et al. Akt2 regulates Rac1 activity in the insulin-dependent signaling pathway leading to GLUT4 translocation to the plasma membrane in skeletal muscle cells. Cell. Signal. 25, 1361-1371 (2013).
    • (2013) Cell. Signal. , vol.25 , pp. 1361-1371
    • Nozaki, S.1
  • 55
    • 84895461940 scopus 로고    scopus 로고
    • A critical role of the small GTPase Rac1 in Akt2-mediated GLUT4 translocation in mouse skeletal muscle
    • Takenaka, N. et al. A critical role of the small GTPase Rac1 in Akt2-mediated GLUT4 translocation in mouse skeletal muscle. FEBS J. 281, 1493-1504 (2014).
    • (2014) FEBS J. , vol.281 , pp. 1493-1504
    • Takenaka, N.1
  • 56
    • 33947578085 scopus 로고    scopus 로고
    • Rab10, a target of the AS160 Rab GAP, is required for insulin-stimulated translocation of GLUT4 to the adipocyte plasma membrane
    • Sano, H. et al. Rab10, a target of the AS160 Rab GAP, is required for insulin-stimulated translocation of GLUT4 to the adipocyte plasma membrane. Cell Metab. 5, 293-303 (2007).
    • (2007) Cell Metab. , vol.5 , pp. 293-303
    • Sano, H.1
  • 57
    • 28544435205 scopus 로고    scopus 로고
    • Full intracellular retention of GLUT4 requires AS160 Rab GTPase activating protein
    • Eguez, L. et al. Full intracellular retention of GLUT4 requires AS160 Rab GTPase activating protein. Cell Metab. 2, 263-272 (2005).
    • (2005) Cell Metab. , vol.2 , pp. 263-272
    • Eguez, L.1
  • 58
    • 84899463909 scopus 로고    scopus 로고
    • Differential actin-regulatory activities of tropomodulin1 and tropomodulin3 with diverse tropomyosin and actin isoforms
    • Yamashiro, S. et al. Differential actin-regulatory activities of tropomodulin1 and tropomodulin3 with diverse tropomyosin and actin isoforms. J. Biol. Chem. 289, 11616-11629 (2014).
    • (2014) J. Biol. Chem. , vol.289 , pp. 11616-11629
    • Yamashiro, S.1
  • 59
    • 0031952055 scopus 로고    scopus 로고
    • Actin depolymerizing factor and cofilin phosphorylation dynamics: Response to signals that regulate neurite extension
    • Meberg, P. J., Ono, S., Minamide, L. S., Takahashi, M. & Bamburg, J. R. Actin depolymerizing factor and cofilin phosphorylation dynamics: response to signals that regulate neurite extension. Cell Motil. Cytoskeleton 39, 172-190 (1998).
    • (1998) Cell Motil. Cytoskeleton , vol.39 , pp. 172-190
    • Meberg, P.J.1    Ono, S.2    Minamide, L.S.3    Takahashi, M.4    Bamburg, J.R.5
  • 60
    • 1342346548 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase-mediated activation of cofilin phosphatase Slingshot and its role for insulin-induced membrane protrusion
    • Nishita, M. et al. Phosphoinositide 3-kinase-mediated activation of cofilin phosphatase Slingshot and its role for insulin-induced membrane protrusion. J. Biol. Chem. 279, 7193-7198 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 7193-7198
    • Nishita, M.1
  • 61
    • 77957735364 scopus 로고    scopus 로고
    • Tropomodulin 1-null mice have a mild spherocytic elliptocytosis with appearance of tropomodulin 3 in red blood cells and disruption of the membrane skeleton
    • Moyer, J. D. et al. Tropomodulin 1-null mice have a mild spherocytic elliptocytosis with appearance of tropomodulin 3 in red blood cells and disruption of the membrane skeleton. Blood 116, 2590-2599 (2010).
    • (2010) Blood , vol.116 , pp. 2590-2599
    • Moyer, J.D.1
  • 62
    • 0037343138 scopus 로고    scopus 로고
    • Specification of actin filament function and molecular composition by tropomyosin isoforms
    • Bryce, N. S. et al. Specification of actin filament function and molecular composition by tropomyosin isoforms. Mol. Biol. Cell 14, 1002-1016 (2003).
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1002-1016
    • Bryce, N.S.1
  • 63
    • 78650056157 scopus 로고    scopus 로고
    • Tropomyosin isoform 3 promotes the formation of filopodia by regulating the recruitment of actin-binding proteins to actin filaments
    • Creed, S. J., Desouza, M., Bamburg, J. R. & Gunning, P. Tropomyosin isoform 3 promotes the formation of filopodia by regulating the recruitment of actin-binding proteins to actin filaments. Exp. Cell Res. 317, 249-261 (2011).
    • (2011) Exp. Cell Res. , vol.317 , pp. 249-261
    • Creed, S.J.1    Desouza, M.2    Bamburg, J.R.3    Gunning, P.4
  • 64
    • 0141545016 scopus 로고    scopus 로고
    • The interaction of tropomodulin with tropomyosin stabilizes thin filaments in cardiac myocytes
    • Mudry, R. E., Perry, C. N., Richards, M., Fowler, V. M. & Gregorio, C. C. The interaction of tropomodulin with tropomyosin stabilizes thin filaments in cardiac myocytes. J. Cell Biol. 162, 1057-1068 (2003).
    • (2003) J. Cell Biol. , vol.162 , pp. 1057-1068
    • Mudry, R.E.1    Perry, C.N.2    Richards, M.3    Fowler, V.M.4    Gregorio, C.C.5
  • 65
    • 20444398071 scopus 로고    scopus 로고
    • Tropomyosin isoforms: Divining rods for actin cytoskeleton function
    • Gunning, P. W., Schevzov, G., Kee, A. J. & Hardeman, E. C. Tropomyosin isoforms: divining rods for actin cytoskeleton function. Trends Cell Biol. 15, 333-341 (2005).
    • (2005) Trends Cell Biol. , vol.15 , pp. 333-341
    • Gunning, P.W.1    Schevzov, G.2    Kee, A.J.3    Hardeman, E.C.4
  • 66
    • 79953794528 scopus 로고    scopus 로고
    • A molecular pathway for myosin II recruitment to stress fibers
    • Tojkander, S. et al. A molecular pathway for myosin II recruitment to stress fibers. Curr. Biol. 21, 539-550 (2011).
    • (2011) Curr. Biol. , vol.21 , pp. 539-550
    • Tojkander, S.1
  • 67
    • 84885134917 scopus 로고    scopus 로고
    • Regulation of myosin light chain kinase during insulin-stimulated glucose uptake in 3T3-L1 adipocytes
    • Woody, S., Stall, R., Ramos, J. & Patel, Y. M. Regulation of myosin light chain kinase during insulin-stimulated glucose uptake in 3T3-L1 adipocytes. PLoS ONE 8, e77248 (2013).
    • (2013) PLoS ONE , vol.8 , pp. e77248
    • Woody, S.1    Stall, R.2    Ramos, J.3    Patel, Y.M.4
  • 68
    • 84872441219 scopus 로고    scopus 로고
    • Regulation of adipogenesis by cytoskeleton remodelling is facilitated by acetyltransferase MEC-17-dependent acetylation of α-tubulin
    • Yang, W. et al. Regulation of adipogenesis by cytoskeleton remodelling is facilitated by acetyltransferase MEC-17-dependent acetylation of α-tubulin. Biochem. J. 449, 605-612 (2013).
    • (2013) Biochem. J. , vol.449 , pp. 605-612
    • Yang, W.1
  • 69
    • 79952441521 scopus 로고    scopus 로고
    • An enzymatic photometric assay for 2-deoxyglucose uptake in insulin-responsive tissues and 3T3-L1 adipocytes
    • Saito, K. et al. An enzymatic photometric assay for 2-deoxyglucose uptake in insulin-responsive tissues and 3T3-L1 adipocytes. Anal. Biochem. 412, 9-17 (2011).
    • (2011) Anal. Biochem. , vol.412 , pp. 9-17
    • Saito, K.1
  • 70
    • 33749489511 scopus 로고    scopus 로고
    • Insulin signaling diverges into Akt-dependent and -independent signals to regulate the recruitment/docking and the fusion of GLUT4 vesicles to the plasma membrane
    • Gonzalez, E. & McGraw, T. E. Insulin signaling diverges into Akt-dependent and -independent signals to regulate the recruitment/docking and the fusion of GLUT4 vesicles to the plasma membrane. Mol. Biol. Cell 17, 4484-4493 (2006).
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4484-4493
    • Gonzalez, E.1    McGraw, T.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.