메뉴 건너뛰기




Volumn 12, Issue 6, 2017, Pages 1703-1710

Phosphorylation Weakens but Does Not Inhibit Membrane Binding and Clustering of K-Ras4B

Author keywords

[No Author keywords available]

Indexed keywords

K RAS PROTEIN; K RAS4B PROTEIN; UNCLASSIFIED DRUG; K-RAS4B PROTEIN, HUMAN; PROTEIN AGGREGATE; PROTEIN P21; SERINE;

EID: 85020924255     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/acschembio.7b00165     Document Type: Article
Times cited : (35)

References (49)
  • 1
    • 0034605862 scopus 로고    scopus 로고
    • Ras - A molecular switch involved in tumor formation
    • Wittinghofer, A. and Waldmann, H. (2000) Ras-A molecular switch involved in tumor formation Angew. Chem., Int. Ed. 39, 4192-4214 10.1002/1521-3773(20001201)39:23<4192::AID-ANIE4192>3.0.CO;2-Y
    • (2000) Angew. Chem., Int. Ed. , vol.39 , pp. 4192-4214
    • Wittinghofer, A.1    Waldmann, H.2
  • 3
    • 84914158670 scopus 로고    scopus 로고
    • The Renaissance of Ras
    • Milroy, L.-G. and Ottmann, C. (2014) The Renaissance of Ras ACS Chem. Biol. 9, 2447-2458 10.1021/cb500555h
    • (2014) ACS Chem. Biol. , vol.9 , pp. 2447-2458
    • Milroy, L.-G.1    Ottmann, C.2
  • 4
    • 84861147473 scopus 로고    scopus 로고
    • A Comprehensive Survey of Ras Mutations in Cancer
    • Prior, I. A., Lewis, P. D., and Mattos, C. (2012) A Comprehensive Survey of Ras Mutations in Cancer Cancer Res. 72, 2457-2467 10.1158/0008-5472.CAN-11-2612
    • (2012) Cancer Res. , vol.72 , pp. 2457-2467
    • Prior, I.A.1    Lewis, P.D.2    Mattos, C.3
  • 5
    • 84928394480 scopus 로고    scopus 로고
    • The Ras Renaissance
    • Ledford, H. (2015) The Ras Renaissance Nature 520, 278-280 10.1038/520278a
    • (2015) Nature , vol.520 , pp. 278-280
    • Ledford, H.1
  • 8
    • 84979976447 scopus 로고    scopus 로고
    • Direct small-molecule inhibitors of KRAS: From structural insights to mechanism-based design
    • Ostrem, J. M. L. and Shokat, K. M. (2016) Direct small-molecule inhibitors of KRAS: from structural insights to mechanism-based design Nat. Rev. Drug Discovery 15, 771-785 10.1038/nrd.2016.139
    • (2016) Nat. Rev. Drug Discovery , vol.15 , pp. 771-785
    • Ostrem, J.M.L.1    Shokat, K.M.2
  • 9
    • 84898606304 scopus 로고    scopus 로고
    • KRas localizes to the plasma membrane by spatial cycles of solubilization, trapping and vesicular transport
    • Schmick, M., Vartak, N., Papke, B., Kovacevic, M., Truxius, D. C., Rossmannek, L., and Bastiaens, P. I. (2014) KRas localizes to the plasma membrane by spatial cycles of solubilization, trapping and vesicular transport Cell 157, 459-471 10.1016/j.cell.2014.02.051
    • (2014) Cell , vol.157 , pp. 459-471
    • Schmick, M.1    Vartak, N.2    Papke, B.3    Kovacevic, M.4    Truxius, D.C.5    Rossmannek, L.6    Bastiaens, P.I.7
  • 10
    • 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 10.1038/nrm1105
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 373-384
    • Hancock, J.F.1
  • 11
    • 27344456331 scopus 로고    scopus 로고
    • H-ras, K-ras, and inner plasma membrane raft proteins operate in nanoclusters with differential dependence on the actin cytoskeleton
    • Plowman, S. J., Muncke, C., Parton, R. G., and Hancock, J. F. (2005) H-ras, K-ras, and inner plasma membrane raft proteins operate in nanoclusters with differential dependence on the actin cytoskeleton Proc. Natl. Acad. Sci. U. S. A. 102, 15500-15505 10.1073/pnas.0504114102
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 15500-15505
    • Plowman, S.J.1    Muncke, C.2    Parton, R.G.3    Hancock, J.F.4
  • 13
    • 84255195028 scopus 로고    scopus 로고
    • Regulating the regulator: Post-translational modification of RAS
    • Ahearn, I. M., Haigis, K., Bar-Sagi, D., and Philips, M. R. (2011) Regulating the regulator: post-translational modification of RAS Nat. Rev. Mol. Cell Biol. 13, 39-51 10.1038/nrm3255
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 39-51
    • Ahearn, I.M.1    Haigis, K.2    Bar-Sagi, D.3    Philips, M.R.4
  • 19
    • 78149467812 scopus 로고    scopus 로고
    • K-Ras4B phosphorylation at Ser181 is inhibited by calmodulin and modulates K-Ras activity and function
    • Alvarez-Moya, B., Lopez-Alcala, C., Drosten, M., Bachs, O., and Agell, N. (2010) K-Ras4B phosphorylation at Ser181 is inhibited by calmodulin and modulates K-Ras activity and function Oncogene 29, 5911-5922 10.1038/onc.2010.298
    • (2010) Oncogene , vol.29 , pp. 5911-5922
    • Alvarez-Moya, B.1    Lopez-Alcala, C.2    Drosten, M.3    Bachs, O.4    Agell, N.5
  • 20
    • 84885436245 scopus 로고    scopus 로고
    • Oncogenic K-ras segregates at spatially distinct plasma membrane signaling platforms according to its phosphorylation status
    • Barcelo, C., Paco, N., Beckett, A. J., Alvarez-Moya, B., Garrido, E., Gelabert, M., Tebar, F., Jaumot, M., Prior, I., and Agell, N. (2013) Oncogenic K-ras segregates at spatially distinct plasma membrane signaling platforms according to its phosphorylation status J. Cell Sci. 126, 4553-4559 10.1242/jcs.123737
    • (2013) J. Cell Sci. , vol.126 , pp. 4553-4559
    • Barcelo, C.1    Paco, N.2    Beckett, A.J.3    Alvarez-Moya, B.4    Garrido, E.5    Gelabert, M.6    Tebar, F.7    Jaumot, M.8    Prior, I.9    Agell, N.10
  • 22
    • 45549094796 scopus 로고    scopus 로고
    • Analysis of K-Ras Phosphorylation, Translocation, and Induction of Apoptosis
    • Quatela, S. E., Sung, P. J., Ahearn, I. M., Bivona, T. G., and Philips, M. R. (2008) Analysis of K-Ras Phosphorylation, Translocation, and Induction of Apoptosis Methods Enzymol. 439, 87-102 10.1016/S0076-6879(07)00407-7
    • (2008) Methods Enzymol. , vol.439 , pp. 87-102
    • Quatela, S.E.1    Sung, P.J.2    Ahearn, I.M.3    Bivona, T.G.4    Philips, M.R.5
  • 23
    • 0027944205 scopus 로고
    • Synthesis of proteins by native chemical ligation
    • Dawson, P. E., Muir, T. W., Clark-Lewis, I., and Kent, S. B. (1994) Synthesis of proteins by native chemical ligation Science 266, 776-779 10.1126/science.7973629
    • (1994) Science , vol.266 , pp. 776-779
    • Dawson, P.E.1    Muir, T.W.2    Clark-Lewis, I.3    Kent, S.B.4
  • 24
    • 61849177109 scopus 로고    scopus 로고
    • Expressed protein ligation (EPL) in the study of signal transduction, ion conduction, and chromatin biology
    • Flavell, R. R. and Muir, T. W. (2009) Expressed protein ligation (EPL) in the study of signal transduction, ion conduction, and chromatin biology Acc. Chem. Res. 42, 107-116 10.1021/ar800129c
    • (2009) Acc. Chem. Res. , vol.42 , pp. 107-116
    • Flavell, R.R.1    Muir, T.W.2
  • 25
    • 84925832272 scopus 로고    scopus 로고
    • Histones: At the crossroads of peptide and protein chemistry
    • Muller, M. M. and Muir, T. W. (2015) Histones: at the crossroads of peptide and protein chemistry Chem. Rev. 115, 2296-2349 10.1021/cr5003529
    • (2015) Chem. Rev. , vol.115 , pp. 2296-2349
    • Muller, M.M.1    Muir, T.W.2
  • 28
    • 84869161983 scopus 로고    scopus 로고
    • Synthesis of peptides containing C-terminal methyl esters using trityl side-chain anchoring: Application to the synthesis of a-factor and a-factor analogs
    • Diaz-Rodriguez, V., Mullen, D. G., Ganusova, E., Becker, J. M., and Distefano, M. D. (2012) Synthesis of peptides containing C-terminal methyl esters using trityl side-chain anchoring: application to the synthesis of a-factor and a-factor analogs Org. Lett. 14, 5648-5651 10.1021/ol302592v
    • (2012) Org. Lett. , vol.14 , pp. 5648-5651
    • Diaz-Rodriguez, V.1    Mullen, D.G.2    Ganusova, E.3    Becker, J.M.4    Distefano, M.D.5
  • 29
    • 0024391460 scopus 로고
    • Total Synthesis of the Lipopeptide a-Mating Factor of Saccharomyces Cerevisiae
    • Xue, C. B., Caldwell, G. A., Becker, J. M., and Naider, F. (1989) Total Synthesis of the Lipopeptide a-Mating Factor of Saccharomyces Cerevisiae Biochem. Biophys. Res. Commun. 162, 253-257 10.1016/0006-291X(89)91989-X
    • (1989) Biochem. Biophys. Res. Commun. , vol.162 , pp. 253-257
    • Xue, C.B.1    Caldwell, G.A.2    Becker, J.M.3    Naider, F.4
  • 30
    • 0029913467 scopus 로고    scopus 로고
    • Differential interaction of the Ras family GTP-binding proteins H-Ras, Rap1A, and R-Ras with the putative effector molecules Raf kinase and Ral-guanine nucleotide exchange factor
    • Herrmann, C., Horn, G., Spaargaren, M., and Wittinghofer, A. (1996) Differential interaction of the Ras family GTP-binding proteins H-Ras, Rap1A, and R-Ras with the putative effector molecules Raf kinase and Ral-guanine nucleotide exchange factor J. Biol. Chem. 271, 6794-6800 10.1074/jbc.271.12.6794
    • (1996) J. Biol. Chem. , vol.271 , pp. 6794-6800
    • Herrmann, C.1    Horn, G.2    Spaargaren, M.3    Wittinghofer, A.4
  • 31
    • 67650725201 scopus 로고    scopus 로고
    • Chapter 1 Protein Phosphorylation by Semisynthesis
    • Szewczuk, L. M., Tarrant, M. K., and Cole, P. A. (2009) Chapter 1 Protein Phosphorylation by Semisynthesis Methods Enzymol. 462, 1-24 10.1016/S0076-6879(09)62001-2
    • (2009) Methods Enzymol. , vol.462 , pp. 1-24
    • Szewczuk, L.M.1    Tarrant, M.K.2    Cole, P.A.3
  • 33
    • 79951559073 scopus 로고    scopus 로고
    • Temperature-pressure phase diagram of a heterogeneous anionic model biomembrane system: Results from a combined calorimetry, spectroscopy and microscopy study
    • Kapoor, S., Werkmueller, A., Denter, C., Zhai, Y., Markgraf, J., Weise, K., Opitz, N., and Winter, R. (2011) Temperature-pressure phase diagram of a heterogeneous anionic model biomembrane system: Results from a combined calorimetry, spectroscopy and microscopy study Biochim. Biophys. Acta, Biomembr. 1808, 1187-1195 10.1016/j.bbamem.2011.01.011
    • (2011) Biochim. Biophys. Acta, Biomembr. , vol.1808 , pp. 1187-1195
    • Kapoor, S.1    Werkmueller, A.2    Denter, C.3    Zhai, Y.4    Markgraf, J.5    Weise, K.6    Opitz, N.7    Winter, R.8
  • 34
    • 84863967918 scopus 로고    scopus 로고
    • Dissociation of the K-Ras4B/PDEdelta complex upon contact with lipid membranes: Membrane delivery instead of extraction
    • Weise, K., Kapoor, S., Werkmuller, A., Mobitz, S., Zimmermann, G., Triola, G., Waldmann, H., and Winter, R. (2012) Dissociation of the K-Ras4B/PDEdelta complex upon contact with lipid membranes: membrane delivery instead of extraction J. Am. Chem. Soc. 134, 11503-11510 10.1021/ja305518h
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 11503-11510
    • Weise, K.1    Kapoor, S.2    Werkmuller, A.3    Mobitz, S.4    Zimmermann, G.5    Triola, G.6    Waldmann, H.7    Winter, R.8
  • 35
    • 84856696581 scopus 로고    scopus 로고
    • Detection of lipid raft domains in neutral and anionic Langmuir monolayers and bilayers of complex lipid composition
    • Evers, F., Jeworrek, C., Weise, K., Tolan, M., and Winter, R. (2012) Detection of lipid raft domains in neutral and anionic Langmuir monolayers and bilayers of complex lipid composition Soft Matter 8, 2170-2175 10.1039/c2sm06835d
    • (2012) Soft Matter , vol.8 , pp. 2170-2175
    • Evers, F.1    Jeworrek, C.2    Weise, K.3    Tolan, M.4    Winter, R.5
  • 36
    • 84887022689 scopus 로고    scopus 로고
    • Rotational and translational dynamics of ras proteins upon binding to model membrane systems
    • Werkmuller, A., Triola, G., Waldmann, H., and Winter, R. (2013) Rotational and translational dynamics of ras proteins upon binding to model membrane systems ChemPhysChem 14, 3698-3705 10.1002/cphc.201300617
    • (2013) ChemPhysChem , vol.14 , pp. 3698-3705
    • Werkmuller, A.1    Triola, G.2    Waldmann, H.3    Winter, R.4
  • 37
    • 84867572593 scopus 로고    scopus 로고
    • The role of G-domain orientation and nucleotide state on the Ras isoform-specific membrane interaction
    • Kapoor, S., Weise, K., Erlkamp, M., Triola, G., Waldmann, H., and Winter, R. (2012) The role of G-domain orientation and nucleotide state on the Ras isoform-specific membrane interaction Eur. Biophys. J. 41, 801-813 10.1007/s00249-012-0841-5
    • (2012) Eur. Biophys. J. , vol.41 , pp. 801-813
    • Kapoor, S.1    Weise, K.2    Erlkamp, M.3    Triola, G.4    Waldmann, H.5    Winter, R.6
  • 38
    • 84928552345 scopus 로고    scopus 로고
    • Chemical tagging and customizing of cellular chromatin states using ultrafast trans-splicing inteins
    • David, Y., Vila-Perello, M., Verma, S., and Muir, T. W. (2015) Chemical tagging and customizing of cellular chromatin states using ultrafast trans-splicing inteins Nat. Chem. 7, 394-402 10.1038/nchem.2224
    • (2015) Nat. Chem. , vol.7 , pp. 394-402
    • David, Y.1    Vila-Perello, M.2    Verma, S.3    Muir, T.W.4
  • 39
    • 13644271605 scopus 로고    scopus 로고
    • Anionic fullerenes, calixarenes, coronenes, and pyrenes as activators of oligo/polyarginines in model membranes and live cells
    • Perret, F., Nishihara, M., Takeuchi, T., Futaki, S., Lazar, A. N., Coleman, A. W., Sakai, N., and Matile, S. (2005) Anionic fullerenes, calixarenes, coronenes, and pyrenes as activators of oligo/polyarginines in model membranes and live cells J. Am. Chem. Soc. 127, 1114-1115 10.1021/ja043633c
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 1114-1115
    • Perret, F.1    Nishihara, M.2    Takeuchi, T.3    Futaki, S.4    Lazar, A.N.5    Coleman, A.W.6    Sakai, N.7    Matile, S.8
  • 42
    • 46149107301 scopus 로고    scopus 로고
    • Electrostatic interactions positively regulate K-Ras nanocluster formation and function
    • Plowman, S. J., Ariotti, N., Goodall, A., Parton, R. G., and Hancock, J. F. (2008) Electrostatic interactions positively regulate K-Ras nanocluster formation and function Mol. Cell. Biol. 28, 4377-4385 10.1128/MCB.00050-08
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 4377-4385
    • Plowman, S.J.1    Ariotti, N.2    Goodall, A.3    Parton, R.G.4    Hancock, J.F.5
  • 43
    • 44849117286 scopus 로고    scopus 로고
    • Identification of essential interacting elements in K-Ras/calmodulin binding and its role in K-Ras localization
    • Lopez-Alcala, C., Alvarez-Moya, B., Villalonga, P., Calvo, M., Bachs, O., and Agell, N. (2008) Identification of essential interacting elements in K-Ras/calmodulin binding and its role in K-Ras localization J. Biol. Chem. 283, 10621-10631 10.1074/jbc.M706238200
    • (2008) J. Biol. Chem. , vol.283 , pp. 10621-10631
    • Lopez-Alcala, C.1    Alvarez-Moya, B.2    Villalonga, P.3    Calvo, M.4    Bachs, O.5    Agell, N.6
  • 44
    • 20644433081 scopus 로고    scopus 로고
    • Effects of farnesol on the physical properties of DMPC membranes
    • Rowat, A. C., Keller, D., and Ipsen, J. H. (2005) Effects of farnesol on the physical properties of DMPC membranes Biochim. Biophys. Acta, Biomembr. 1713, 29-39 10.1016/j.bbamem.2005.04.014
    • (2005) Biochim. Biophys. Acta, Biomembr. , vol.1713 , pp. 29-39
    • Rowat, A.C.1    Keller, D.2    Ipsen, J.H.3
  • 45
    • 3042751258 scopus 로고    scopus 로고
    • Farnesylated peptides in model membranes: A biophysical investigation
    • Rowat, A. C., Brask, J., Sparrman, T., Jensen, K. J., Lindblom, G., and Ipsen, J. H. (2004) Farnesylated peptides in model membranes: a biophysical investigation Eur. Biophys. J. 33, 562-563 10.1007/s00249-004-0429-9
    • (2004) Eur. Biophys. J. , vol.33 , pp. 562-563
    • Rowat, A.C.1    Brask, J.2    Sparrman, T.3    Jensen, K.J.4    Lindblom, G.5    Ipsen, J.H.6
  • 47
    • 84881043798 scopus 로고    scopus 로고
    • Differential scanning calorimetry of protein-lipid interactions
    • Canadas, O. and Casals, C. (2013) Differential scanning calorimetry of protein-lipid interactions Methods Mol. Biol. 974, 55-71 10.1007/978-1-62703-275-9-4
    • (2013) Methods Mol. Biol. , vol.974 , pp. 55-71
    • Canadas, O.1    Casals, C.2
  • 48
    • 23244457196 scopus 로고    scopus 로고
    • Ras diffusion is sensitive to plasma membrane viscosity
    • Goodwin, J. S., Drake, K. R., Remmert, C. L., and Kenworthy, A. K. (2005) Ras diffusion is sensitive to plasma membrane viscosity Biophys. J. 89, 1398-1410 10.1529/biophysj.104.055640
    • (2005) Biophys. J. , vol.89 , pp. 1398-1410
    • Goodwin, J.S.1    Drake, K.R.2    Remmert, C.L.3    Kenworthy, A.K.4
  • 49
    • 84921819284 scopus 로고    scopus 로고
    • Solanum Nigrum Polysaccharide (SNL) Extract Effects in Transplanted Tumor-bearing Mice - Erythrocyte Membrane Fluidity and Blocking of Functions
    • Yuan, H.-L., Liu, X.-L., and Liu, Y.-J. (2015) Solanum Nigrum Polysaccharide (SNL) Extract Effects in Transplanted Tumor-bearing Mice-Erythrocyte Membrane Fluidity and Blocking of Functions Asian Pac. J. Cancer Prev. 15, 10469-10473 10.7314/APJCP.2014.15.23.10469
    • (2015) Asian Pac. J. Cancer Prev. , vol.15 , pp. 10469-10473
    • Yuan, H.-L.1    Liu, X.-L.2    Liu, Y.-J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.