메뉴 건너뛰기




Volumn 111, Issue 1, 2016, Pages 113-122

Regulation of K-Ras4B Membrane Binding by Calmodulin

Author keywords

[No Author keywords available]

Indexed keywords

CALMODULIN; PROTEIN BINDING; PROTEIN P21;

EID: 84992513190     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2016.05.042     Document Type: Article
Times cited : (43)

References (58)
  • 2
    • 0037542854 scopus 로고    scopus 로고
    • Ras proteins: different signals from different locations
    • 2 Hancock, J.F., Ras proteins: different signals from different locations. Nat. Rev. Mol. Cell Biol. 4 (2003), 373–384.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 373-384
    • Hancock, J.F.1
  • 3
    • 0034605862 scopus 로고    scopus 로고
    • Ras—a molecular switch involved in tumor formation
    • 3 Wittinghofer, A., Waldmann, H., Ras—a molecular switch involved in tumor formation. Angew. Chem. Int. Ed. Engl. 39 (2000), 4192–4214.
    • (2000) Angew. Chem. Int. Ed. Engl. , vol.39 , pp. 4192-4214
    • Wittinghofer, A.1    Waldmann, H.2
  • 4
    • 0025740753 scopus 로고
    • The structure of Ras protein: a model for a universal molecular switch
    • 4 Wittinghofer, A., Pai, E.F., The structure of Ras protein: a model for a universal molecular switch. Trends Biochem. Sci. 16 (1991), 382–387.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 382-387
    • Wittinghofer, A.1    Pai, E.F.2
  • 5
    • 28844509531 scopus 로고    scopus 로고
    • K-ras as a target for cancer therapy
    • 5 Friday, B.B., Adjei, A.A., K-ras as a target for cancer therapy. Biochim. Biophys. Acta 1756 (2005), 127–144.
    • (2005) Biochim. Biophys. Acta , vol.1756 , pp. 127-144
    • Friday, B.B.1    Adjei, A.A.2
  • 6
    • 0024376173 scopus 로고
    • ras oncogenes in human cancer: a review
    • 6 Bos, J.L., ras oncogenes in human cancer: a review. Cancer Res. 49 (1989), 4682–4689.
    • (1989) Cancer Res. , vol.49 , pp. 4682-4689
    • Bos, J.L.1
  • 7
    • 84861147473 scopus 로고    scopus 로고
    • A comprehensive survey of Ras mutations in cancer
    • 7 Prior, I.A., Lewis, P.D., Mattos, C., A comprehensive survey of Ras mutations in cancer. Cancer Res. 72 (2012), 2457–2467.
    • (2012) Cancer Res. , vol.72 , pp. 2457-2467
    • Prior, I.A.1    Lewis, P.D.2    Mattos, C.3
  • 8
    • 0025013547 scopus 로고
    • A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21ras to the plasma membrane
    • 8 Hancock, J.F., Paterson, H., Marshall, C.J., A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21ras to the plasma membrane. Cell 63 (1990), 133–139.
    • (1990) Cell , vol.63 , pp. 133-139
    • Hancock, J.F.1    Paterson, H.2    Marshall, C.J.3
  • 9
    • 0028584355 scopus 로고
    • Polylysine domain of K-ras 4B protein is crucial for malignant transformation
    • 9 Jackson, J.H., Li, J.W., et al., Cochrane, C.G., Polylysine domain of K-ras 4B protein is crucial for malignant transformation. Proc. Natl. Acad. Sci. USA 91 (1994), 12730–12734.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12730-12734
    • Jackson, J.H.1    Li, J.W.2    Cochrane, C.G.3
  • 11
    • 0021170342 scopus 로고
    • The p21 ras C-terminus is required for transformation and membrane association
    • 11 Willumsen, B.M., Christensen, A., et al., Lowy, D.R., The p21 ras C-terminus is required for transformation and membrane association. Nature 310 (1984), 583–586.
    • (1984) Nature , vol.310 , pp. 583-586
    • Willumsen, B.M.1    Christensen, A.2    Lowy, D.R.3
  • 12
    • 84856492497 scopus 로고    scopus 로고
    • The GDI-like solubilizing factor PDEδ sustains the spatial organization and signalling of Ras family proteins
    • 12 Chandra, A., Grecco, H.E., et al., Bastiaens, P.I., The GDI-like solubilizing factor PDEδ sustains the spatial organization and signalling of Ras family proteins. Nat. Cell Biol. 14 (2011), 148–158.
    • (2011) Nat. Cell Biol. , vol.14 , pp. 148-158
    • Chandra, A.1    Grecco, H.E.2    Bastiaens, P.I.3
  • 13
    • 84898606304 scopus 로고    scopus 로고
    • KRas localizes to the plasma membrane by spatial cycles of solubilization, trapping and vesicular transport
    • 13 Schmick, M., Vartak, N., et al., Bastiaens, P.I., KRas localizes to the plasma membrane by spatial cycles of solubilization, trapping and vesicular transport. Cell 157 (2014), 459–471.
    • (2014) Cell , vol.157 , pp. 459-471
    • Schmick, M.1    Vartak, N.2    Bastiaens, P.I.3
  • 14
    • 81355127367 scopus 로고    scopus 로고
    • Arl2-GTP and Arl3-GTP regulate a GDI-like transport system for farnesylated cargo
    • 14 Ismail, S.A., Chen, Y.X., et al., Wittinghofer, A., Arl2-GTP and Arl3-GTP regulate a GDI-like transport system for farnesylated cargo. Nat. Chem. Biol. 7 (2011), 942–949.
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 942-949
    • Ismail, S.A.1    Chen, Y.X.2    Wittinghofer, A.3
  • 16
    • 0034790751 scopus 로고    scopus 로고
    • Calmodulin binds to K-Ras, but not to H- or N-Ras, and modulates its downstream signaling
    • 16 Villalonga, P., López-Alcalá, C., et al., Agell, N., Calmodulin binds to K-Ras, but not to H- or N-Ras, and modulates its downstream signaling. Mol. Cell. Biol. 21 (2001), 7345–7354.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7345-7354
    • Villalonga, P.1    López-Alcalá, C.2    Agell, N.3
  • 17
    • 68849095670 scopus 로고    scopus 로고
    • The hypervariable region of K-Ras4B is responsible for its specific interactions with calmodulin
    • 17 Abraham, S.J., Nolet, R.P., et al., Gaponenko, V., The hypervariable region of K-Ras4B is responsible for its specific interactions with calmodulin. Biochemistry 48 (2009), 7575–7583.
    • (2009) Biochemistry , vol.48 , pp. 7575-7583
    • Abraham, S.J.1    Nolet, R.P.2    Gaponenko, V.3
  • 18
    • 0029149085 scopus 로고
    • Molecular and structural basis of target recognition by calmodulin
    • 18 Crivici, A., Ikura, M., Molecular and structural basis of target recognition by calmodulin. Annu. Rev. Biophys. Biomol. Struct. 24 (1995), 85–116.
    • (1995) Annu. Rev. Biophys. Biomol. Struct. , vol.24 , pp. 85-116
    • Crivici, A.1    Ikura, M.2
  • 20
    • 0024213513 scopus 로고
    • Structure of calmodulin refined at 2.2 A resolution
    • 20 Babu, Y.S., Bugg, C.E., Cook, W.J., Structure of calmodulin refined at 2.2 A resolution. J. Mol. Biol. 204 (1988), 191–204.
    • (1988) J. Mol. Biol. , vol.204 , pp. 191-204
    • Babu, Y.S.1    Bugg, C.E.2    Cook, W.J.3
  • 21
    • 0029160568 scopus 로고
    • Calcium-induced conformational transition revealed by the solution structure of apo calmodulin
    • 21 Zhang, M., Tanaka, T., Ikura, M., Calcium-induced conformational transition revealed by the solution structure of apo calmodulin. Nat. Struct. Biol. 2 (1995), 758–767.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 758-767
    • Zhang, M.1    Tanaka, T.2    Ikura, M.3
  • 22
    • 0037318056 scopus 로고    scopus 로고
    • Novel aspects of calmodulin target recognition and activation
    • 22 Vetter, S.W., Leclerc, E., Novel aspects of calmodulin target recognition and activation. Eur. J. Biochem. 270 (2003), 404–414.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 404-414
    • Vetter, S.W.1    Leclerc, E.2
  • 23
    • 0037155689 scopus 로고    scopus 로고
    • Calmodulin in action: diversity in target recognition and activation mechanisms
    • 23 Hoeflich, K.P., Ikura, M., Calmodulin in action: diversity in target recognition and activation mechanisms. Cell 108 (2002), 739–742.
    • (2002) Cell , vol.108 , pp. 739-742
    • Hoeflich, K.P.1    Ikura, M.2
  • 26
    • 78649263874 scopus 로고    scopus 로고
    • Multiple cellular proteins modulate the dynamics of K-ras association with the plasma membrane
    • 26 Bhagatji, P., Leventis, R., et al., Silvius, J.R., Multiple cellular proteins modulate the dynamics of K-ras association with the plasma membrane. Biophys. J. 99 (2010), 3327–3335.
    • (2010) Biophys. J. , vol.99 , pp. 3327-3335
    • Bhagatji, P.1    Leventis, R.2    Silvius, J.R.3
  • 27
    • 79959988123 scopus 로고    scopus 로고
    • Both the C-terminal polylysine region and the farnesylation of K-RasB are important for its specific interaction with calmodulin
    • 27 Wu, L.J., Xu, L.R., et al., Liang, Y., Both the C-terminal polylysine region and the farnesylation of K-RasB are important for its specific interaction with calmodulin. PLoS One, 6, 2011, e21929.
    • (2011) PLoS One , vol.6 , pp. e21929
    • Wu, L.J.1    Xu, L.R.2    Liang, Y.3
  • 28
    • 44849117286 scopus 로고    scopus 로고
    • Identification of essential interacting elements in K-Ras/calmodulin binding and its role in K-Ras localization
    • 28 Lopez-Alcalá, C., Alvarez-Moya, B., et al., Agell, N., Identification of essential interacting elements in K-Ras/calmodulin binding and its role in K-Ras localization. J. Biol. Chem. 283 (2008), 10621–10631.
    • (2008) J. Biol. Chem. , vol.283 , pp. 10621-10631
    • Lopez-Alcalá, C.1    Alvarez-Moya, B.2    Agell, N.3
  • 29
    • 84863967918 scopus 로고    scopus 로고
    • Dissociation of the K-Ras4B/PDEδ complex upon contact with lipid membranes: membrane delivery instead of extraction
    • 29 Weise, K., Kapoor, S., et al., Winter, R., Dissociation of the K-Ras4B/PDEδ complex upon contact with lipid membranes: membrane delivery instead of extraction. J. Am. Chem. Soc. 134 (2012), 11503–11510.
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 11503-11510
    • Weise, K.1    Kapoor, S.2    Winter, R.3
  • 30
  • 31
    • 79851483766 scopus 로고    scopus 로고
    • Membrane-mediated induction and sorting of K-Ras microdomain signaling platforms
    • 31 Weise, K., Kapoor, S., et al., Winter, R., Membrane-mediated induction and sorting of K-Ras microdomain signaling platforms. J. Am. Chem. Soc. 133 (2011), 880–887.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 880-887
    • Weise, K.1    Kapoor, S.2    Winter, R.3
  • 32
    • 77952761642 scopus 로고    scopus 로고
    • Influence of the lipid anchor motif of N-ras on the interaction with lipid membranes: a surface plasmon resonance study
    • 32 Gohlke, A., Triola, G., et al., Winter, R., Influence of the lipid anchor motif of N-ras on the interaction with lipid membranes: a surface plasmon resonance study. Biophys. J. 98 (2010), 2226–2235.
    • (2010) Biophys. J. , vol.98 , pp. 2226-2235
    • Gohlke, A.1    Triola, G.2    Winter, R.3
  • 33
    • 63149129301 scopus 로고    scopus 로고
    • Influence of the lipidation motif on the partitioning and association of N-Ras in model membrane subdomains
    • 33 Weise, K., Triola, G., et al., Winter, R., Influence of the lipidation motif on the partitioning and association of N-Ras in model membrane subdomains. J. Am. Chem. Soc. 131 (2009), 1557–1564.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 1557-1564
    • Weise, K.1    Triola, G.2    Winter, R.3
  • 34
    • 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
    • 34 Plowman, S.J., Muncke, C., et al., Hancock, J.F., H-ras, K-ras, and inner plasma membrane raft proteins operate in nanoclusters with differential dependence on the actin cytoskeleton. Proc. Natl. Acad. Sci. USA 102 (2005), 15500–15505.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 15500-15505
    • Plowman, S.J.1    Muncke, C.2    Hancock, J.F.3
  • 35
    • 62149129986 scopus 로고    scopus 로고
    • Compartmentalized signalling: Ras proteins and signalling nanoclusters
    • 35 Omerovic, J., Prior, I.A., Compartmentalized signalling: Ras proteins and signalling nanoclusters. FEBS J. 276 (2009), 1817–1825.
    • (2009) FEBS J. , vol.276 , pp. 1817-1825
    • Omerovic, J.1    Prior, I.A.2
  • 36
    • 0034304851 scopus 로고    scopus 로고
    • Lipid rafts and signal transduction
    • 36 Simons, K., Toomre, D., Lipid rafts and signal transduction. Nat. Rev. Mol. Cell Biol. 1 (2000), 31–39.
    • (2000) Nat. Rev. Mol. Cell Biol. , vol.1 , pp. 31-39
    • Simons, K.1    Toomre, D.2
  • 37
    • 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
    • 37 Kapoor, S., Werkmüller, A., et al., Winter, R., Temperature-pressure phase diagram of a heterogeneous anionic model biomembrane system: results from a combined calorimetry, spectroscopy and microscopy study. Biochim. Biophys. Acta 1808 (2011), 1187–1195.
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 1187-1195
    • Kapoor, S.1    Werkmüller, A.2    Winter, R.3
  • 38
    • 84856696581 scopus 로고    scopus 로고
    • Detection of lipid raft domains in neutral and anionic Langmuir monolayers and bilayers of complex lipid composition
    • 38 Evers, F., Jeworrek, C., et al., Winter, R., Detection of lipid raft domains in neutral and anionic Langmuir monolayers and bilayers of complex lipid composition. Soft Matter 8 (2012), 2170–2175.
    • (2012) Soft Matter , vol.8 , pp. 2170-2175
    • Evers, F.1    Jeworrek, C.2    Winter, R.3
  • 39
    • 84904160692 scopus 로고    scopus 로고
    • Interaction of the human N-Ras protein with lipid raft model membranes of varying degrees of complexity
    • 39 Vogel, A., Nikolaus, J., et al., Huster, D., Interaction of the human N-Ras protein with lipid raft model membranes of varying degrees of complexity. Biol. Chem. 395 (2014), 779–789.
    • (2014) Biol. Chem. , vol.395 , pp. 779-789
    • Vogel, A.1    Nikolaus, J.2    Huster, D.3
  • 40
    • 70350604271 scopus 로고    scopus 로고
    • The lipid modifications of Ras that sense membrane environments and induce local enrichment
    • 40 Vogel, A., Reuther, G., et al., Huster, D., The lipid modifications of Ras that sense membrane environments and induce local enrichment. Angew. Chem. Int. Ed. Engl. 48 (2009), 8784–8787.
    • (2009) Angew. Chem. Int. Ed. Engl. , vol.48 , pp. 8784-8787
    • Vogel, A.1    Reuther, G.2    Huster, D.3
  • 41
    • 0034089628 scopus 로고    scopus 로고
    • Surface plasmon resonance analysis of dynamic biological interactions with biomaterials
    • 41 Green, R.J., Frazier, R.A., et al., Tendler, S.J., Surface plasmon resonance analysis of dynamic biological interactions with biomaterials. Biomaterials 21 (2000), 1823–1835.
    • (2000) Biomaterials , vol.21 , pp. 1823-1835
    • Green, R.J.1    Frazier, R.A.2    Tendler, S.J.3
  • 42
    • 0037326012 scopus 로고    scopus 로고
    • Surface plasmon resonance spectroscopy in the study of membrane-mediated cell signalling
    • 42 Mozsolits, H., Thomas, W.G., Aguilar, M.I., Surface plasmon resonance spectroscopy in the study of membrane-mediated cell signalling. J. Pept. Sci. 9 (2003), 77–89.
    • (2003) J. Pept. Sci. , vol.9 , pp. 77-89
    • Mozsolits, H.1    Thomas, W.G.2    Aguilar, M.I.3
  • 43
    • 33746728985 scopus 로고    scopus 로고
    • Surface plasmon resonance in protein-membrane interactions
    • 43 Besenicar, M., Macek, P., et al., Anderluh, G., Surface plasmon resonance in protein-membrane interactions. Chem. Phys. Lipids 141 (2006), 169–178.
    • (2006) Chem. Phys. Lipids , vol.141 , pp. 169-178
    • Besenicar, M.1    Macek, P.2    Anderluh, G.3
  • 44
    • 84867572593 scopus 로고    scopus 로고
    • The role of G-domain orientation and nucleotide state on the Ras isoform-specific membrane interaction
    • 44 Kapoor, S., Weise, K., et al., Winter, R., The role of G-domain orientation and nucleotide state on the Ras isoform-specific membrane interaction. Eur. Biophys. J. 41 (2012), 801–813.
    • (2012) Eur. Biophys. J. , vol.41 , pp. 801-813
    • Kapoor, S.1    Weise, K.2    Winter, R.3
  • 45
    • 84856005311 scopus 로고    scopus 로고
    • Revealing conformational substates of lipidated N-Ras protein by pressure modulation
    • 45 Kapoor, S., Triola, G., et al., Winter, R., Revealing conformational substates of lipidated N-Ras protein by pressure modulation. Proc. Natl. Acad. Sci. USA 109 (2012), 460–465.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 460-465
    • Kapoor, S.1    Triola, G.2    Winter, R.3
  • 46
    • 0020491146 scopus 로고
    • 2+-dependent interaction of 5-dimethylaminonaphthalene-1-sulfonyl-calmodulin with cyclic nucleotide phosphodiesterase, calcineurin, and troponin I
    • 2+-dependent interaction of 5-dimethylaminonaphthalene-1-sulfonyl-calmodulin with cyclic nucleotide phosphodiesterase, calcineurin, and troponin I. J. Biol. Chem. 257 (1982), 10638–10643.
    • (1982) J. Biol. Chem. , vol.257 , pp. 10638-10643
    • Kincaid, R.L.1    Vaughan, M.2    Tkachuk, V.A.3
  • 47
    • 0028232698 scopus 로고
    • Resolution of structural changes associated with calcium activation of calmodulin using frequency domain fluorescence spectroscopy
    • 47 Yao, Y., Schöneich, C., Squier, T.C., Resolution of structural changes associated with calcium activation of calmodulin using frequency domain fluorescence spectroscopy. Biochemistry 33 (1994), 7797–7810.
    • (1994) Biochemistry , vol.33 , pp. 7797-7810
    • Yao, Y.1    Schöneich, C.2    Squier, T.C.3
  • 48
    • 0026007188 scopus 로고
    • Time-resolved fluorescence spectroscopy. Applications to calmodulin
    • 48 Anderson, S.R., Time-resolved fluorescence spectroscopy. Applications to calmodulin. J. Biol. Chem. 266 (1991), 11405–11408.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11405-11408
    • Anderson, S.R.1
  • 49
    • 84887022689 scopus 로고    scopus 로고
    • Rotational and translational dynamics of ras proteins upon binding to model membrane systems
    • 49 Werkmüller, A., Triola, G., et al., Winter, R., Rotational and translational dynamics of ras proteins upon binding to model membrane systems. ChemPhysChem 14 (2013), 3698–3705.
    • (2013) ChemPhysChem , vol.14 , pp. 3698-3705
    • Werkmüller, A.1    Triola, G.2    Winter, R.3
  • 50
    • 0032555491 scopus 로고    scopus 로고
    • Calmodulin inhibitor W13 induces sustained activation of ERK2 and expression of p21(cip1)
    • 50 Bosch, M., Gil, J., et al., Agell, N., Calmodulin inhibitor W13 induces sustained activation of ERK2 and expression of p21(cip1). J. Biol. Chem. 273 (1998), 22145–22150.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22145-22150
    • Bosch, M.1    Gil, J.2    Agell, N.3
  • 51
    • 84947713840 scopus 로고    scopus 로고
    • K-ras promotes tumorigenicity through suppression of non-canonical Wnt signaling
    • 51 Wang, M.T., Holderfield, M., et al., McCormick, F., K-ras promotes tumorigenicity through suppression of non-canonical Wnt signaling. Cell 163 (2015), 1237–1251.
    • (2015) Cell , vol.163 , pp. 1237-1251
    • Wang, M.T.1    Holderfield, M.2    McCormick, F.3
  • 52
    • 0028028022 scopus 로고
    • Phosphorylation, high ionic strength, and calmodulin reverse the binding of MARCKS to phospholipid vesicles
    • 52 Kim, J., Shishido, T., et al., McLaughlin, S., Phosphorylation, high ionic strength, and calmodulin reverse the binding of MARCKS to phospholipid vesicles. J. Biol. Chem. 269 (1994), 28214–28219.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28214-28219
    • Kim, J.1    Shishido, T.2    McLaughlin, S.3
  • 53
    • 28444477387 scopus 로고    scopus 로고
    • Plasma membrane phosphoinositide organization by protein electrostatics
    • 53 McLaughlin, S., Murray, D., Plasma membrane phosphoinositide organization by protein electrostatics. Nature 438 (2005), 605–611.
    • (2005) Nature , vol.438 , pp. 605-611
    • McLaughlin, S.1    Murray, D.2
  • 55
    • 0020997959 scopus 로고
    • A continuously variable frequency cross-correlation phase fluorometer with picosecond resolution
    • 55 Gratton, E., Limkeman, M., A continuously variable frequency cross-correlation phase fluorometer with picosecond resolution. Biophys. J. 44 (1983), 315–324.
    • (1983) Biophys. J. , vol.44 , pp. 315-324
    • Gratton, E.1    Limkeman, M.2
  • 58
    • 0035964342 scopus 로고    scopus 로고
    • Electrostatics of nanosystems: application to microtubules and the ribosome
    • 58 Baker, N.A., Sept, D., et al., McCammon, J.A., Electrostatics of nanosystems: application to microtubules and the ribosome. Proc. Natl. Acad. Sci. USA 98 (2001), 10037–10041.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10037-10041
    • Baker, N.A.1    Sept, D.2    McCammon, J.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.