메뉴 건너뛰기




Volumn 8, Issue 1, 2012, Pages 102-110

FERM domain interaction with myosin negatively regulates FAK in cardiomyocyte hypertrophy

Author keywords

[No Author keywords available]

Indexed keywords

ERYTHROCYTE BAND 4.1 PROTEIN; EZRIN; FOCAL ADHESION KINASE; MOESIN; MYOSIN; RADIXIN;

EID: 83655201165     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.717     Document Type: Article
Times cited : (15)

References (39)
  • 1
    • 11244258882 scopus 로고    scopus 로고
    • Focal adhesion kinase: In command and control of cell motility
    • DOI 10.1038/nrm1549
    • Mitra, S.K., Hanson, D.A. & Schlaepfer, D.D. Focal adhesion kinase: in command and control of cell motility. Nat. Rev. Mol. Cell Biol. 6, 56-68 (2005). (Pubitemid 40064899)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.1 , pp. 56-68
    • Mitra, S.K.1    Hanson, D.A.2    Schlaepfer, D.D.3
  • 2
    • 77951184829 scopus 로고    scopus 로고
    • Cellular functions of FAK kinases: Insight into molecular mechanisms and novel functions
    • Schaller, M.D. Cellular functions of FAK kinases: insight into molecular mechanisms and novel functions. J. Cell Sci. 123, 1007-1013 (2010).
    • (2010) J. Cell Sci. , vol.123 , pp. 1007-1013
    • Schaller, M.D.1
  • 6
    • 76849100707 scopus 로고    scopus 로고
    • Focal adhesion kinase: A prominent determinant in breast cancer initiation, progression and metastasis
    • Luo, M. & Guan, J.L. Focal adhesion kinase: a prominent determinant in breast cancer initiation, progression and metastasis. Cancer Lett. 289, 127-139 (2010).
    • (2010) Cancer Lett. , vol.289 , pp. 127-139
    • Luo, M.1    Guan, J.L.2
  • 7
    • 33748741079 scopus 로고    scopus 로고
    • Myocyte-restricted focal adhesion kinase deletion attenuates pressure overload-induced hypertrophy
    • DiMichele, L.A., et al. Myocyte-restricted focal adhesion kinase deletion attenuates pressure overload-induced hypertrophy. Circ. Res. 99, 636-645 (2006).
    • (2006) Circ. Res. , vol.99 , pp. 636-645
    • Dimichele, L.A.1
  • 8
    • 0042266791 scopus 로고    scopus 로고
    • Focal adhesion kinase is activated and mediates the early hypertrophic response to stretch in cardiac myocytes
    • DOI 10.1161/01.RES.0000081595.25297.1B
    • Torsoni, A.S., Constancio, S.S., Nadruz, W. Jr., Hanks, S.K. & Franchini, K.G. Focal adhesion kinase is activated and mediates the early hypertrophic response to stretch in cardiac myocytes. Circ. Res. 93, 140-147 (2003). (Pubitemid 36919701)
    • (2003) Circulation Research , vol.93 , Issue.2 , pp. 140-147
    • Torsoni, A.S.1    Constancio, S.S.2    Nadruz Jr., W.3    Hanks, S.K.4    Franchini, K.G.5
  • 9
    • 0037160058 scopus 로고    scopus 로고
    • The N termini of focal adhesion kinase family members regulate substrate phosphorylation, localization, and cell morphology
    • DOI 10.1074/jbc.M201779200
    • Dunty, J.M. & Schaller, M.D. The N termini of focal adhesion kinase family members regulate substrate phosphorylation, localization, and cell morphology. J. Biol. Chem. 277, 45644-45654 (2002). (Pubitemid 36159176)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.47 , pp. 45644-45654
    • Dunty, J.M.1    Schaller, M.D.2
  • 11
    • 34250026140 scopus 로고    scopus 로고
    • Structural basis for the autoinhibition of focal adhesion kinase
    • DOI 10.1016/j.cell.2007.05.041, PII S0092867407006800
    • Lietha, D., et al. Structural basis for the autoinhibition of focal adhesion kinase. Cell 129, 1177-1187 (2007). (Pubitemid 46891044)
    • (2007) Cell , vol.129 , Issue.6 , pp. 1177-1187
    • Lietha, D.1    Cai, X.2    Ceccarelli, D.F.J.3    Li, Y.4    Schaller, M.D.5    Eck, M.J.6
  • 14
    • 0037509990 scopus 로고    scopus 로고
    • Focal adhesion kinase: The first ten years
    • DOI 10.1242/jcs.00373
    • Parsons, J.T. Focal adhesion kinase: the first ten years. J. Cell Sci. 116, 1409-1416 (2003). (Pubitemid 36527488)
    • (2003) Journal of Cell Science , vol.116 , Issue.8 , pp. 1409-1416
    • Parsons, J.T.1
  • 15
    • 0028350859 scopus 로고
    • Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src
    • Schaller, M.D., et al. Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src. Mol. Cell. Biol. 14, 1680-1688 (1994).
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1680-1688
    • Schaller, M.D.1
  • 17
    • 0028877919 scopus 로고
    • Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: A role for Src family kinases
    • Calalb, M.B., Polte, T.R. & Hanks, S.K. Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: a role for Src family kinases. Mol. Cell. Biol. 15, 954-963 (1995).
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 954-963
    • Calalb, M.B.1    Polte, T.R.2    Hanks, S.K.3
  • 20
    • 33745468872 scopus 로고    scopus 로고
    • Direct interaction of focal adhesion kinase (FAK) with Met is required for FAK to promote hepatocyte growth factor-induced cell invasion
    • Chen, S.Y. & Chen, H.C. Direct interaction of focal adhesion kinase (FAK) with Met is required for FAK to promote hepatocyte growth factor-induced cell invasion. Mol. Cell. Biol. 26, 5155-5167 (2006).
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 5155-5167
    • Chen, S.Y.1    Chen, H.C.2
  • 23
    • 0034705523 scopus 로고    scopus 로고
    • A role for focal adhesion kinase in phenylephrine-induced hypertrophy of rat ventricular cardiomyocytes
    • DOI 10.1074/jbc.M909099199
    • Taylor, J.M., Rovin, J.D. & Parsons, J.T. A role for focal adhesion kinase in phenylephrine-induced hypertrophy of rat ventricular cardiomyocytes. J. Biol. Chem. 275, 19250-19257 (2000). (Pubitemid 30422897)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.25 , pp. 19250-19257
    • Taylor, J.M.1    Rovin, J.D.2    Parsons, J.T.3
  • 26
    • 11844275921 scopus 로고    scopus 로고
    • Targeting to C-terminal myosin heavy chain may explain mechanotransduction involving focal adhesion kinase in cardiac myocytes
    • DOI 10.1161/01.RES.0000152390.99806.A5
    • Fonseca, P.M., et al. Targeting to C-terminal myosin heavy chain may explain mechanotransduction involving focal adhesion kinase in cardiac myocytes. Circ. Res. 96, 73-81 (2005). (Pubitemid 40095756)
    • (2005) Circulation Research , vol.96 , Issue.1 , pp. 73-81
    • Fonseca, P.M.1    Inoue, R.Y.2    Kobarg, C.B.3    Crosara-Alberto, D.P.4    Kobarg, J.5    Franchini, K.G.6
  • 27
    • 0345169163 scopus 로고    scopus 로고
    • Small-angle scattering: A view on the properties, structures and structural changes of biological macromolecules in solution
    • DOI 10.1017/S0033583503003871
    • Koch, M.H., Vachette, P. & Svergun, D.I. Small-angle scattering: a view on the properties, structures and structural changes of biological macromolecules in solution. Q. Rev. Biophys. 36, 147-227 (2003). (Pubitemid 37493573)
    • (2003) Quarterly Reviews of Biophysics , vol.36 , Issue.2 , pp. 147-227
    • Koch, M.H.J.1    Vachette, P.2    Svergun, D.I.3
  • 28
    • 0041932511 scopus 로고    scopus 로고
    • Additive protection of the ischemic heart ex vivo by combined treatment with δ-protein kinase C inhibitor and ε-protein kinase C activator
    • DOI 10.1161/01.CIR.0000081943.93653.73
    • Inagaki, K., Hahn, H.S., Dorn, G.W. II. & Mochly-Rosen, D. Additive protection of the ischemic heart ex vivo by combined treatment with delta-protein kinase C inhibitor and epsilon-protein kinase C activator. Circulation 108, 869-875 (2003). (Pubitemid 37022131)
    • (2003) Circulation , vol.108 , Issue.7 , pp. 869-875
    • Inagaki, K.1    Hahn, H.S.2    Dorn II, G.W.3    Mochly-Rosen, D.4
  • 30
    • 54449101472 scopus 로고    scopus 로고
    • Shp2 negatively regulates growth in cardiomyocytes by controlling focal adhesion kinase/Src and mTOR pathways
    • Marin, T.M., et al. Shp2 negatively regulates growth in cardiomyocytes by controlling focal adhesion kinase/Src and mTOR pathways. Circ. Res. 103, 813-824 (2008).
    • (2008) Circ. Res. , vol.103 , pp. 813-824
    • Marin, T.M.1
  • 31
    • 0034634653 scopus 로고    scopus 로고
    • Integrin activation and focal complex formation in cardiac hypertrophy
    • Laser, M., et al. Integrin activation and focal complex formation in cardiac hypertrophy. J. Biol. Chem. 275, 35624-35630 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 35624-35630
    • Laser, M.1
  • 32
    • 0029150292 scopus 로고
    • Focal adhesion kinase and paxillin bind to peptides mimicking beta integrin cytoplasmic domains
    • Schaller, M.D., Otey, C.A., Hildebrand, J.D. & Parsons, J.T. Focal adhesion kinase and paxillin bind to peptides mimicking beta integrin cytoplasmic domains. J. Cell Biol. 130, 1181-1187 (1995).
    • (1995) J. Cell Biol. , vol.130 , pp. 1181-1187
    • Schaller, M.D.1    Otey, C.A.2    Hildebrand, J.D.3    Parsons, J.T.4
  • 33
    • 76149098520 scopus 로고    scopus 로고
    • Identification of cross-linked peptides by high-resolution precursor ion scan
    • Iglesias, A.H., Santos, L.F. & Gozzo, F.C. Identification of cross-linked peptides by high-resolution precursor ion scan. Anal. Chem. 82, 909-916 (2010).
    • (2010) Anal. Chem. , vol.82 , pp. 909-916
    • Iglesias, A.H.1    Santos, L.F.2    Gozzo, F.C.3
  • 34
    • 33747840389 scopus 로고    scopus 로고
    • GRAMM-X public web server for protein-protein docking
    • DOI 10.1093/nar/gkl206
    • Tovchigrechko, A. & Vakser, I.A. GRAMM-X public web server for protein-protein docking. Nucleic Acids Res. 34, W310-W314 (2006). (Pubitemid 44529784)
    • (2006) Nucleic Acids Research , vol.34 , Issue.WEB. SERV. ISS.
    • Tovchigrechko, A.1    Vakser, I.A.2
  • 35
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • DOI 10.1107/S0021889895007047
    • Svergun, D.I., Barberato, C. & Koch, M.H.J. CRYSOL-a program to evaluate x-ray solution scattering of biological macromolecule from atomic coordinate. J. Appl. Crystallogr. 28, 768-773 (1995). (Pubitemid 3014671)
    • (1995) Journal of Applied Crystallography , vol.28 , Issue.6 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.3
  • 36
    • 58949104029 scopus 로고    scopus 로고
    • Human FEZ1 has characteristics of a natively unfolded protein and dimerizes in solution
    • Lanza, D.C., et al. Human FEZ1 has characteristics of a natively unfolded protein and dimerizes in solution. Proteins 74, 104-121 (2009).
    • (2009) Proteins , vol.74 , pp. 104-121
    • Lanza, D.C.1
  • 37
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • DOI 10.1529/biophysj.105.064154
    • Petoukhov, M.V. & Svergun, D.I. Global rigid body modeling of macromolecular complexes against small-angle scattering data. Biophys. J. 89, 1237-1250 (2005). (Pubitemid 41099005)
    • (2005) Biophysical Journal , vol.89 , Issue.2 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 38
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov, V.V. & Svergun, D.I. Uniqueness of ab initio shape determination in small-angle scattering. J. Appl. Crystallogr. 36, 860-864 (2003).
    • (2003) J. Appl. Crystallogr. , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 39
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and low-resolution structural models
    • DOI 10.1107/S0021889800014126
    • Kozin, P.V. & Svergun, D.I. Automated matching of high-and low-resolution structural models. J. Appl. Crystallogr. 34, 33-41 (2001). (Pubitemid 32151714)
    • (2001) Journal of Applied Crystallography , vol.34 , Issue.1 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.