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Volumn 123, Issue 1, 2010, Pages 51-61

Integrin activation by Fam38A uses a novel mechanism of R-Ras targeting to the endoplasmic reticulum

Author keywords

Calpain; Cell adhesion; Endoplasmic reticulum; Integrins; R Ras

Indexed keywords

BETA1 INTEGRIN; CALPAIN; DUAL SPECIFICITY PHOSPHATASE 2; FAM 38A PROTEIN; INTEGRIN; MEMBRANE PROTEIN; RAS PROTEIN; SMALL INTERFERING RNA; TALIN; UNCLASSIFIED DRUG;

EID: 72449161735     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.056424     Document Type: Article
Times cited : (160)

References (52)
  • 1
    • 33646806089 scopus 로고    scopus 로고
    • The small GTPase R-Ras regulates organization of actin and drives membrane protrusions through the activity of PLCepsilon
    • Ada-Nguema, A. S., Xenias, H., Hofman, J. M., Wiggins, C. H., Sheetz, M. P. and Keely, P. J. (2006). The small GTPase R-Ras regulates organization of actin and drives membrane protrusions through the activity of PLCepsilon. J. Cell Sci. 119, 1307-1319.
    • (2006) J. Cell Sci , vol.119 , pp. 1307-1319
    • Ada-Nguema, A.S.1    Xenias, H.2    Hofman, J.M.3    Wiggins, C.H.4    Sheetz, M.P.5    Keely, P.J.6
  • 2
    • 1242316976 scopus 로고    scopus 로고
    • Calpain-1 regulates Bax and subsequent Smac-dependent caspase-3 activation in neutrophil apoptosis
    • Altznauer, F., Conus, S., Cavalli, A., Folkers, G. and Simon, H. U. (2004). Calpain-1 regulates Bax and subsequent Smac-dependent caspase-3 activation in neutrophil apoptosis. J. Biol. Chem. 279, 5947-5957.
    • (2004) J. Biol. Chem , vol.279 , pp. 5947-5957
    • Altznauer, F.1    Conus, S.2    Cavalli, A.3    Folkers, G.4    Simon, H.U.5
  • 3
    • 0034116930 scopus 로고    scopus 로고
    • Disruption of the murine calpain small subunit gene, Capn4: Calpain is essential for embryonic development but not for cell growth and division
    • Arthur, J. S., Elce, J. S., Hegadorn, C., Williams, K. and Greer, P. A. (2000). Disruption of the murine calpain small subunit gene, Capn4: calpain is essential for embryonic development but not for cell growth and division. Mol. Cell. Biol. 20, 4474-4481.
    • (2000) Mol. Cell. Biol , vol.20 , pp. 4474-4481
    • Arthur, J.S.1    Elce, J.S.2    Hegadorn, C.3    Williams, K.4    Greer, P.A.5
  • 4
    • 0036711804 scopus 로고    scopus 로고
    • Bhatt, A., Kaverina, I., Otey, C. and Huttenlocher, A. (2002). Regulation of focal complex composition and disass.e.m.bly by the calcium-dependent protease calpain. J. Cell Sci. 115, 3415-3425.
    • Bhatt, A., Kaverina, I., Otey, C. and Huttenlocher, A. (2002). Regulation of focal complex composition and disass.e.m.bly by the calcium-dependent protease calpain. J. Cell Sci. 115, 3415-3425.
  • 5
    • 33748948921 scopus 로고    scopus 로고
    • Calpain 2 and Src dependence distinguishes mesenchymal and amoeboid modes of tumour cell invasion: A link to integrin function
    • Carragher, N. O., Walker, S. M., Scott Carragher, L. A., Harris, F., Sawyer, T. K., Brunton, V. G., Ozanne, B. W. and Frame, M. C. (2006). Calpain 2 and Src dependence distinguishes mesenchymal and amoeboid modes of tumour cell invasion: a link to integrin function. Oncogene 25, 5726-5740.
    • (2006) Oncogene , vol.25 , pp. 5726-5740
    • Carragher, N.O.1    Walker, S.M.2    Scott Carragher, L.A.3    Harris, F.4    Sawyer, T.K.5    Brunton, V.G.6    Ozanne, B.W.7    Frame, M.C.8
  • 6
    • 0036091925 scopus 로고    scopus 로고
    • Chiu, V. K., Bivona, T., Hach, A., Sajous, J. B., Silletti, J., Wiener, H., Johnson, R. L., 2nd, Cox, A. D. and Philips, M. R. (2002). Ras signalling on the endoplasmic reticulum and the Golgi. Nat. Cell Biol. 4, 343-350.
    • Chiu, V. K., Bivona, T., Hach, A., Sajous, J. B., Silletti, J., Wiener, H., Johnson, R. L., 2nd, Cox, A. D. and Philips, M. R. (2002). Ras signalling on the endoplasmic reticulum and the Golgi. Nat. Cell Biol. 4, 343-350.
  • 8
    • 0031814839 scopus 로고    scopus 로고
    • Integrins and cardiovascular disease
    • Clemetson, K. J. and Clemetson, J. M. (1998). Integrins and cardiovascular disease. Cell Mol. Life Sci. 54, 502-513.
    • (1998) Cell Mol. Life Sci , vol.54 , pp. 502-513
    • Clemetson, K.J.1    Clemetson, J.M.2
  • 10
    • 28844491633 scopus 로고    scopus 로고
    • Determination of peptide substrate specificity for mu-calpain by a peptide library-based approach: The importance of primed side interactions
    • Cuerrier, D., Moldoveanu, T. and Davies, P. L. (2005). Determination of peptide substrate specificity for mu-calpain by a peptide library-based approach: the importance of primed side interactions. J. Biol. Chem. 280, 40632-40641.
    • (2005) J. Biol. Chem , vol.280 , pp. 40632-40641
    • Cuerrier, D.1    Moldoveanu, T.2    Davies, P.L.3
  • 12
    • 0030710958 scopus 로고    scopus 로고
    • Complementation of dominant suppression implicates CD98 in integrin activation
    • Fenczik, C. A., Sethi, T., Ramos, J. W., Hughes, P. E. and Ginsberg, M. H. (1997). Complementation of dominant suppression implicates CD98 in integrin activation. Nature 390, 81-85.
    • (1997) Nature , vol.390 , pp. 81-85
    • Fenczik, C.A.1    Sethi, T.2    Ramos, J.W.3    Hughes, P.E.4    Ginsberg, M.H.5
  • 15
    • 0038049137 scopus 로고    scopus 로고
    • Tumour-cell invasion and migration: Diversity and escape mechanisms
    • Friedl, P. and Wolf, K. (2003). Tumour-cell invasion and migration: diversity and escape mechanisms. Nat. Rev. Cancer 3, 362-374.
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 362-374
    • Friedl, P.1    Wolf, K.2
  • 16
    • 0033758751 scopus 로고    scopus 로고
    • N-terminal cleavage of bax by calpain generates a potent proapoptotic 18-kDa fragment that promotes bcl-2-independent cytochrome c release and apoptotic cell death
    • Gao, G. and Dou, Q. P. (2000). N-terminal cleavage of bax by calpain generates a potent proapoptotic 18-kDa fragment that promotes bcl-2-independent cytochrome c release and apoptotic cell death. J. Cell Biochem. 80, 53-72.
    • (2000) J. Cell Biochem , vol.80 , pp. 53-72
    • Gao, G.1    Dou, Q.P.2
  • 17
    • 0035968342 scopus 로고    scopus 로고
    • Membrane proximal ERK signalling is required for M-calpain activation downstream of epidermal growth factor receptor signalling
    • Glading, A., Uberall, F., Keyse, S. M., Lauffenburger, D. A. and Wells, A. (2001). Membrane proximal ERK signalling is required for M-calpain activation downstream of epidermal growth factor receptor signalling. J. Biol. Chem. 276, 23341-23348.
    • (2001) J. Biol. Chem , vol.276 , pp. 23341-23348
    • Glading, A.1    Uberall, F.2    Keyse, S.M.3    Lauffenburger, D.A.4    Wells, A.5
  • 18
    • 33748561168 scopus 로고    scopus 로고
    • RLIP76 (RalBP1) is an R-Ras effector that mediates adhesion-dependent Rac activation and cell migration
    • Goldfinger, L. E., Ptak, C., Jeffery, E. D., Shabanowitz, J., Hunt, D. F. and Ginsberg, M. H. (2006). RLIP76 (RalBP1) is an R-Ras effector that mediates adhesion-dependent Rac activation and cell migration. J. Cell Biol. 174, 877-888.
    • (2006) J. Cell Biol , vol.174 , pp. 877-888
    • Goldfinger, L.E.1    Ptak, C.2    Jeffery, E.D.3    Shabanowitz, J.4    Hunt, D.F.5    Ginsberg, M.H.6
  • 19
    • 5044238876 scopus 로고    scopus 로고
    • Integrin signalling during tumour progression
    • Guo, W. and Giancotti, F. G. (2004). Integrin signalling during tumour progression. Nat. Rev. Mol. Cell. Biol. 5, 816-826.
    • (2004) Nat. Rev. Mol. Cell. Biol , vol.5 , pp. 816-826
    • Guo, W.1    Giancotti, F.G.2
  • 20
    • 0037542854 scopus 로고    scopus 로고
    • Ras proteins: Different signals from different locations
    • Hancock, J. F. (2003). Ras proteins: different signals from different locations. Nat. Rev. Mol. Cell. Biol. 4, 373-384.
    • (2003) Nat. Rev. Mol. Cell. Biol , vol.4 , pp. 373-384
    • Hancock, J.F.1
  • 21
    • 0037182753 scopus 로고    scopus 로고
    • R-Ras C-terminal sequences are sufficient to confer R-Ras specificity to H-Ras
    • Hansen, M., Rusyn, E. V., Hughes, P. E., Ginsberg, M. H., Cox, A. D. and Willumsen, B. M. (2002). R-Ras C-terminal sequences are sufficient to confer R-Ras specificity to H-Ras. Oncogene 21, 4448-4461.
    • (2002) Oncogene , vol.21 , pp. 4448-4461
    • Hansen, M.1    Rusyn, E.V.2    Hughes, P.E.3    Ginsberg, M.H.4    Cox, A.D.5    Willumsen, B.M.6
  • 22
    • 0037310529 scopus 로고    scopus 로고
    • Ras redux: Rethinking how and where Ras acts
    • Hingorani, S. R. and Tuveson, D. A. (2003). Ras redux: rethinking how and where Ras acts. Curr. Opin. Genet. Dev. 13, 6-13.
    • (2003) Curr. Opin. Genet. Dev , vol.13 , pp. 6-13
    • Hingorani, S.R.1    Tuveson, D.A.2
  • 23
    • 33748685968 scopus 로고    scopus 로고
    • ECM overrides DNA damage-induced cell cycle arrest and apoptosis in small-cell lung cancer cells through beta1 integrin-dependent activation of PI3-kinase
    • Hodkinson, P. S., Elliott, T., Wong, W. S., Rintoul, R. C., Mackinnon, A. C., Haslett, C. and Sethi, T. (2006). ECM overrides DNA damage-induced cell cycle arrest and apoptosis in small-cell lung cancer cells through beta1 integrin-dependent activation of PI3-kinase. Cell Death Differ. 13, 1776-1788.
    • (2006) Cell Death Differ , vol.13 , pp. 1776-1788
    • Hodkinson, P.S.1    Elliott, T.2    Wong, W.S.3    Rintoul, R.C.4    Mackinnon, A.C.5    Haslett, C.6    Sethi, T.7
  • 25
    • 18244390470 scopus 로고    scopus 로고
    • The unique N-terminus of R-ras is required for Rac activation and precise regulation of cell migration
    • Holly, S. P., Larson, M. K. and Parise, L. V. (2005). The unique N-terminus of R-ras is required for Rac activation and precise regulation of cell migration. Mol. Biol. Cell 16, 2458-2469.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 2458-2469
    • Holly, S.P.1    Larson, M.K.2    Parise, L.V.3
  • 26
    • 0036488589 scopus 로고    scopus 로고
    • Role of integrins in cell invasion and migration
    • Hood, J. D. and Cheresh, D. A. (2002). Role of integrins in cell invasion and migration. Nat. Rev. Cancer 2, 91-100.
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 91-100
    • Hood, J.D.1    Cheresh, D.A.2
  • 27
    • 0030909050 scopus 로고    scopus 로고
    • Suppression of integrin activation: A novel function of a Ras/Raf-initiated MAP kinase pathway
    • Hughes, P. E., Renshaw, M. W., Pfaff, M., Forsyth, J., Keivens, V. M., Schwartz, M. A. and Ginsberg, M. H. (1997). Suppression of integrin activation: a novel function of a Ras/Raf-initiated MAP kinase pathway. Cell 88, 521-530.
    • (1997) Cell , vol.88 , pp. 521-530
    • Hughes, P.E.1    Renshaw, M.W.2    Pfaff, M.3    Forsyth, J.4    Keivens, V.M.5    Schwartz, M.A.6    Ginsberg, M.H.7
  • 28
    • 0036327732 scopus 로고    scopus 로고
    • Suppression of integrin activation by activated Ras or Raf does not correlate with bulk activation of ERK MAP kinase
    • Hughes, P. E., Oertli, B., Hansen, M., Chou, F. L., Willumsen, B. M. and Ginsberg, M. H. (2002). Suppression of integrin activation by activated Ras or Raf does not correlate with bulk activation of ERK MAP kinase. Mol. Biol. Cell 13, 2256-2265.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2256-2265
    • Hughes, P.E.1    Oertli, B.2    Hansen, M.3    Chou, F.L.4    Willumsen, B.M.5    Ginsberg, M.H.6
  • 29
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signalling machines
    • Hynes, R. O. (2002). Integrins: bidirectional, allosteric signalling machines. Cell 110, 673-687.
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 30
    • 58149279827 scopus 로고    scopus 로고
    • Activation of the MAPK module from different spatial locations generates distinct system outputs
    • Inder, K., Harding, A., Plowman, S. J., Philips, M. R., Parton, R. G. and Hancock, J. F. (2008). Activation of the MAPK module from different spatial locations generates distinct system outputs. Mol. Biol. Cell 19, 4776-4784.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4776-4784
    • Inder, K.1    Harding, A.2    Plowman, S.J.3    Philips, M.R.4    Parton, R.G.5    Hancock, J.F.6
  • 34
    • 15844363687 scopus 로고    scopus 로고
    • Activated conformations of very late activation integrins detected by a group of antibodies (HUTS) specific for a novel regulatory region (355-425) of the common beta 1 chain
    • Luque, A., Gomez, M., Puzon, W., Takada, Y., Sanchez-Madrid, F. and Cabanas, C. (1996). Activated conformations of very late activation integrins detected by a group of antibodies (HUTS) specific for a novel regulatory region (355-425) of the common beta 1 chain. J. Biol. Chem. 271, 11067-11075.
    • (1996) J. Biol. Chem , vol.271 , pp. 11067-11075
    • Luque, A.1    Gomez, M.2    Puzon, W.3    Takada, Y.4    Sanchez-Madrid, F.5    Cabanas, C.6
  • 35
    • 0031038131 scopus 로고    scopus 로고
    • R-Ras can activate the phosphoinositide 3-kinase but not the MAP kinase arm of the Ras effector pathways
    • Marte, B. M., Rodriguez-Viciana, P., Wennstrom, S., Warne, P. H. and Downward, J. (1997). R-Ras can activate the phosphoinositide 3-kinase but not the MAP kinase arm of the Ras effector pathways. Curr. Biol. 7, 63-70.
    • (1997) Curr. Biol , vol.7 , pp. 63-70
    • Marte, B.M.1    Rodriguez-Viciana, P.2    Wennstrom, S.3    Warne, P.H.4    Downward, J.5
  • 36
    • 9444240314 scopus 로고    scopus 로고
    • Invadolysin: A novel, conserved metalloprotease links mitotic structural rearrangements with cell migration
    • McHugh, B., Krause, S. A., Yu, B., Deans, A. M., Heasman, S., McLaughlin, P. and Heck, M. M. (2004). Invadolysin: a novel, conserved metalloprotease links mitotic structural rearrangements with cell migration. J. Cell Biol. 167, 673-686.
    • (2004) J. Cell Biol , vol.167 , pp. 673-686
    • McHugh, B.1    Krause, S.A.2    Yu, B.3    Deans, A.M.4    Heasman, S.5    McLaughlin, P.6    Heck, M.M.7
  • 39
    • 0032545497 scopus 로고    scopus 로고
    • The death effector domain of PEA-15 is involved in its regulation of integrin activation
    • Ramos, J. W., Kojima, T. K., Hughes, P. E., Fenczik, C. A. and Ginsberg, M. H. (1998). The death effector domain of PEA-15 is involved in its regulation of integrin activation. J. Biol. Chem. 273, 33897-33900.
    • (1998) J. Biol. Chem , vol.273 , pp. 33897-33900
    • Ramos, J.W.1    Kojima, T.K.2    Hughes, P.E.3    Fenczik, C.A.4    Ginsberg, M.H.5
  • 40
    • 0027381394 scopus 로고
    • Calpain activity increases in hepatocytes following addition of ATP. Demonstration by a novel fluorescent approach
    • Rosser, B. G., Powers, S. P. and Gores, G. J. (1993). Calpain activity increases in hepatocytes following addition of ATP. Demonstration by a novel fluorescent approach. J. Biol. Chem. 268, 23593-235600.
    • (1993) J. Biol. Chem , vol.268 , pp. 23593-235600
    • Rosser, B.G.1    Powers, S.P.2    Gores, G.J.3
  • 41
    • 33747785243 scopus 로고    scopus 로고
    • A novel membrane protein, encoded by the gene covering KIAA0233, is transcriptionally induced in senile plaque-associated astrocytes
    • Satoh, K., Hata, M., Takahara, S., Tsuzaki, H., Yokota, H., Akatsu, H., Yamamoto, T., Kosaka, K. and Yamada, T. (2006). A novel membrane protein, encoded by the gene covering KIAA0233, is transcriptionally induced in senile plaque-associated astrocytes. Brain Res. 1108, 19-27.
    • (2006) Brain Res , vol.1108 , pp. 19-27
    • Satoh, K.1    Hata, M.2    Takahara, S.3    Tsuzaki, H.4    Yokota, H.5    Akatsu, H.6    Yamamoto, T.7    Kosaka, K.8    Yamada, T.9
  • 42
    • 33646822656 scopus 로고    scopus 로고
    • Integrin alpha2-mediated ERK and calpain activation play a critical role in cell adhesion and motility via focal adhesion kinase signalling: Identification of a novel signalling pathway
    • Sawhney, R. S., Cookson, M. M., Omar, Y., Hauser, J. and Brattain, M. G. (2006). Integrin alpha2-mediated ERK and calpain activation play a critical role in cell adhesion and motility via focal adhesion kinase signalling: identification of a novel signalling pathway. J. Biol. Chem. 281, 8497-8510.
    • (2006) J. Biol. Chem , vol.281 , pp. 8497-8510
    • Sawhney, R.S.1    Cookson, M.M.2    Omar, Y.3    Hauser, J.4    Brattain, M.G.5
  • 43
    • 0030661566 scopus 로고    scopus 로고
    • Integrins, oncogenes, and anchorage independence
    • Schwartz, M. A. (1997). Integrins, oncogenes, and anchorage independence. J. Cell Biol. 139, 575-578.
    • (1997) J. Cell Biol , vol.139 , pp. 575-578
    • Schwartz, M.A.1
  • 44
    • 0032979447 scopus 로고    scopus 로고
    • The small GTP-binding protein R-Ras can influence integrin activation by antagonizing a Ras/Raf-initiated integrin suppression pathway
    • Sethi, T., Ginsberg, M. H., Downward, J. and Hughes, P. E. (1999). The small GTP-binding protein R-Ras can influence integrin activation by antagonizing a Ras/Raf-initiated integrin suppression pathway. Mol. Biol. Cell 10, 1799-1809.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1799-1809
    • Sethi, T.1    Ginsberg, M.H.2    Downward, J.3    Hughes, P.E.4
  • 45
  • 46
    • 0031569532 scopus 로고    scopus 로고
    • Calpain, an upstream regulator of thymocyte apoptosis
    • Squier, M. K. and Cohen, J. J. (1997). Calpain, an upstream regulator of thymocyte apoptosis. J. Immunol. 158, 3690-3697.
    • (1997) J. Immunol , vol.158 , pp. 3690-3697
    • Squier, M.K.1    Cohen, J.J.2
  • 48
    • 0021170342 scopus 로고
    • The p21 ras C-terminus is required for transformation and membrane association
    • Willumsen, B. M., Christensen, A., Hubbert, N. L., Papageorge, A. G. and Lowy, D. R. (1984). The p21 ras C-terminus is required for transformation and membrane association. Nature 310, 583-586.
    • (1984) Nature , vol.310 , pp. 583-586
    • Willumsen, B.M.1    Christensen, A.2    Hubbert, N.L.3    Papageorge, A.G.4    Lowy, D.R.5
  • 50
    • 11144322264 scopus 로고    scopus 로고
    • R-Ras controls membrane protrusion and cell migration through the spatial regulation of Rac and Rho
    • Wozniak, M. A., Kwong, L., Chodniewicz, D., Klemke, R. L. and Keely, P. J. (2005). R-Ras controls membrane protrusion and cell migration through the spatial regulation of Rac and Rho. Mol. Biol. Cell 16, 84-96.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 84-96
    • Wozniak, M.A.1    Kwong, L.2    Chodniewicz, D.3    Klemke, R.L.4    Keely, P.J.5
  • 51
    • 33747754138 scopus 로고    scopus 로고
    • The R-Ras GTPase mediates cross talk between estrogen and insulin signalling in breast cancer cells
    • Yu, Y., Hao, Y. and Feig, L. A. (2006). The R-Ras GTPase mediates cross talk between estrogen and insulin signalling in breast cancer cells. Mol. Cell. Biol. 26, 6372-6380.
    • (2006) Mol. Cell. Biol , vol.26 , pp. 6372-6380
    • Yu, Y.1    Hao, Y.2    Feig, L.A.3


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