메뉴 건너뛰기




Volumn 5, Issue 255, 2012, Pages

A CC-SAM, for coiled coil-sterile α motif, domain targets the scaffold KSR-1 to specific sites in the plasma membrane

Author keywords

[No Author keywords available]

Indexed keywords

B RAF KINASE; DIMYRISTOYLPHOSPHATIDYLGLYCEROL; GROWTH FACTOR; KINASE SUPPRESSOR OF RAS 1; PHOSPHOLIPID; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG;

EID: 84871527806     PISSN: 19450877     EISSN: 19379145     Source Type: Journal    
DOI: 10.1126/scisignal.2003289     Document Type: Article
Times cited : (23)

References (46)
  • 1
    • 34248597065 scopus 로고    scopus 로고
    • Differential regulation and properties of MAPKs
    • M. Raman, W. Chen, M. H. Cobb, Differential regulation and properties of MAPKs. Oncogene 26, 3100-3112 (2007).
    • (2007) Oncogene , vol.26 , pp. 3100-3112
    • Raman, M.1    Chen, W.2    Cobb, M.H.3
  • 2
    • 0037453510 scopus 로고    scopus 로고
    • Assembly of cell regulatory systems through protein interaction domains
    • T. Pawson, P. Nash, Assembly of cell regulatory systems through protein interaction domains. Science 300, 445-452 (2003).
    • (2003) Science , vol.300 , pp. 445-452
    • Pawson, T.1    Nash, P.2
  • 3
    • 0031043776 scopus 로고    scopus 로고
    • Signal transduction from multiple Ras effectors
    • M. E. Katz, F. McCormick, Signal transduction from multiple Ras effectors. Curr. Opin. Genet. Dev. 7, 75-79 (1997).
    • (1997) Curr. Opin. Genet. Dev. , vol.7 , pp. 75-79
    • Katz, M.E.1    McCormick, F.2
  • 4
    • 66349132474 scopus 로고    scopus 로고
    • Lipid binding domains: More than simple lipid effectors
    • R. V. Stahelin, Lipid binding domains: More than simple lipid effectors. J. Lipid Res. 50 (suppl.), S299-S304 (2009).
    • (2009) J. Lipid Res. , vol.50 , Issue.SUPPL.
    • Stahelin, R.V.1
  • 5
    • 0034698068 scopus 로고    scopus 로고
    • Elucidation of binding determinants and functional consequences of Ras/Raf-cysteine-rich domain interactions
    • J. G. Williams, J. K. Drugan, G. S. Yi, G. J. Clark, C. J. Der, S. L. Campbell, Elucidation of binding determinants and functional consequences of Ras/Raf-cysteine-rich domain interactions. J. Biol. Chem. 275, 22172-22179 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 22172-22179
    • Williams, J.G.1    Drugan, J.K.2    Yi, G.S.3    Clark, G.J.4    Der, C.J.5    Campbell, S.L.6
  • 8
    • 0029588204 scopus 로고
    • The ksr-1 gene encodes a novel protein kinase involved in Ras-mediated signaling in C. elegans
    • K. Kornfeld, D. B. Hom, H. R. Horvitz, The ksr-1 gene encodes a novel protein kinase involved in Ras-mediated signaling in C. elegans. Cell 83, 903-913 (1995).
    • (1995) Cell , vol.83 , pp. 903-913
    • Kornfeld, K.1    Hom, D.B.2    Horvitz, H.R.3
  • 9
    • 0029559183 scopus 로고
    • The C. elegans ksr-1 gene encodes a novel raf-related kinase involved in Ras-mediated signal transduction
    • M. Sundaram, M. Han, The C. elegans ksr-1 gene encodes a novel raf-related kinase involved in Ras-mediated signal transduction. Cell 83, 889-901 (1995).
    • (1995) Cell , vol.83 , pp. 889-901
    • Sundaram, M.1    Han, M.2
  • 10
    • 67449164361 scopus 로고    scopus 로고
    • KSR2 is a calcineurin substrate that promotes ERK cascade activation in response to calcium signals
    • M. K. Dougherty, D. A. Ritt, M. Zhou, S. I. Specht, D. M. Monson, T. D. Veenstra, D. K. Morrison, KSR2 is a calcineurin substrate that promotes ERK cascade activation in response to calcium signals. Mol. Cell 34, 652-662 (2009).
    • (2009) Mol. Cell , vol.34 , pp. 652-662
    • Dougherty, M.K.1    Ritt, D.A.2    Zhou, M.3    Specht, S.I.4    Monson, D.M.5    Veenstra, T.D.6    Morrison, D.K.7
  • 11
    • 0036301210 scopus 로고    scopus 로고
    • Solution structure and functional analysis of the cysteine-rich C1 domain of kinase suppressor of ras (KSR)
    • M. Zhou, D. A. Horita, D. S. Waugh, R. A. Byrd, D. K. Morrison, Solution structure and functional analysis of the cysteine-rich C1 domain of kinase suppressor of ras (KSR). J. Mol. Biol. 315, 435-446 (2002).
    • (2002) J. Mol. Biol. , vol.315 , pp. 435-446
    • Zhou, M.1    Horita, D.A.2    Waugh, D.S.3    Byrd, R.A.4    Morrison, D.K.5
  • 15
    • 0035930343 scopus 로고    scopus 로고
    • C-TAK1 regulates Ras signaling by phosphorylating the MAPK scaffold, KSR1
    • J. Müller, S. Ory, T. Copeland, H. Piwnica-Worms, D. K. Morrison, C-TAK1 regulates Ras signaling by phosphorylating the MAPK scaffold, KSR1. Mol. Cell 8, 983-993 (2001).
    • (2001) Mol. Cell , vol.8 , pp. 983-993
    • Müller, J.1    Ory, S.2    Copeland, T.3    Piwnica-Worms, H.4    Morrison, D.K.5
  • 19
    • 0345306620 scopus 로고    scopus 로고
    • Binding of the C-terminal sterile a motif (SAM) domain of human p73 to lipid membranes
    • F. N. Barrera, J. A. Poveda, J. M. González-Ros, J. L. Neira, Binding of the C-terminal sterile a motif (SAM) domain of human p73 to lipid membranes. J. Biol. Chem. 278, 46878-46885 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 46878-46885
    • Barrera, F.N.1    Poveda, J.A.2    González-Ros, J.M.3    Neira, J.L.4
  • 20
    • 30344442873 scopus 로고    scopus 로고
    • The many faces of SAM
    • F. Qiao, J. U. Bowie, The many faces of SAM. Sci. STKE 2005, re7 (2005).
    • (2005) Sci. STKE , vol.2005
    • Qiao, F.1    Bowie, J.U.2
  • 21
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • L. Holm, P. Rosenström, Dali server: Conservation mapping in 3D. Nucleic Acids Res. 38, W545-W549 (2010).
    • (2010) Nucleic Acids Res. , vol.38
    • Holm, L.1    Rosenström, P.2
  • 22
    • 0032948019 scopus 로고    scopus 로고
    • The crystal structure of an Eph receptor SAM domain reveals a mechanism for modular dimerization
    • D. Stapleton, I. Balan, T. Pawson, F. Sicheri, The crystal structure of an Eph receptor SAM domain reveals a mechanism for modular dimerization. Nat. Struct. Biol. 6, 44-49 (1999).
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 44-49
    • Stapleton, D.1    Balan, I.2    Pawson, T.3    Sicheri, F.4
  • 24
    • 0030832045 scopus 로고    scopus 로고
    • A domain shared by the Polycomb group proteins Scm and ph mediates heterotypic and homotypic interactions
    • A. J. Peterson, M. Kyba, D. Bornemann, K. Morgan, H. W. Brock, J. Simon, A domain shared by the Polycomb group proteins Scm and ph mediates heterotypic and homotypic interactions. Mol. Cell. Biol. 17, 6683-6692 (1997).
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6683-6692
    • Peterson, A.J.1    Kyba, M.2    Bornemann, D.3    Morgan, K.4    Brock, H.W.5    Simon, J.6
  • 25
    • 0031022602 scopus 로고    scopus 로고
    • SAM as a protein interaction domain involved in developmental regulation
    • J. Schultz, C. P. Ponting, K. Hofmann, P. Bork, SAM as a protein interaction domain involved in developmental regulation. Protein Sci. 6, 249-253 (1997).
    • (1997) Protein Sci. , vol.6 , pp. 249-253
    • Schultz, J.1    Ponting, C.P.2    Hofmann, K.3    Bork, P.4
  • 26
    • 0033575719 scopus 로고    scopus 로고
    • Solution structure of a conserved C-terminal domain of p73 with structural homology to the SAM domain
    • S. W. Chi, A. Ayed, C. H. Arrowsmith, Solution structure of a conserved C-terminal domain of p73 with structural homology to the SAM domain. EMBO J. 18, 4438-4445 (1999).
    • (1999) EMBO J. , vol.18 , pp. 4438-4445
    • Chi, S.W.1    Ayed, A.2    Arrowsmith, C.H.3
  • 27
    • 34248574289 scopus 로고    scopus 로고
    • Solution structures, dynamics, and lipid-binding of the sterile a-motif domain of the deleted in liver cancer 2
    • H. Li, K. L. Fung, D. Y. Jin, S. S. Chung, Y. P. Ching, I. O. Ng, K. H. Sze, B. C. Ko, H. Sun, Solution structures, dynamics, and lipid-binding of the sterile a-motif domain of the deleted in liver cancer 2. Proteins 67, 1154-1166 (2007).
    • (2007) Proteins , vol.67 , pp. 1154-1166
    • Li, H.1    Fung, K.L.2    Jin, D.Y.3    Chung, S.S.4    Ching, Y.P.5    Ng, I.O.6    Sze, K.H.7    Ko, B.C.8    Sun, H.9
  • 29
    • 30044450420 scopus 로고    scopus 로고
    • Comparison of structure and dynamics of micelle-bound human α-synuclein and Parkinson disease variants
    • T. S. Ulmer, A. Bax, Comparison of structure and dynamics of micelle-bound human α-synuclein and Parkinson disease variants. J. Biol. Chem. 280, 43179-43187 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 43179-43187
    • Ulmer, T.S.1    Bax, A.2
  • 31
    • 70349745154 scopus 로고    scopus 로고
    • Recent advances in the application of solution NMR spectroscopy to multi-span integral membrane proteins
    • H. J. Kim, S. C. Howell, W. D. Van Horn, Y. H. Jeon, C. R. Sanders, Recent advances in the application of solution NMR spectroscopy to multi-span integral membrane proteins. Prog. Nucl. Magn. Reson. Spectrosc. 55, 335-360 (2009).
    • (2009) Prog. Nucl. Magn. Reson. Spectrosc. , vol.55 , pp. 335-360
    • Kim, H.J.1    Howell, S.C.2    Van Horn, W.D.3    Jeon, Y.H.4    Sanders, C.R.5
  • 32
    • 33746217557 scopus 로고    scopus 로고
    • Solution NMR of membrane proteins: Practice and challenges
    • C. R. Sanders, F. Sönnichsen, Solution NMR of membrane proteins: Practice and challenges. Magn. Reson. Chem. 44 Spec. No, S24-S40 (2006).
    • (2006) Magn. Reson. Chem. , vol.44 , Issue.SPEC. NO
    • Sanders, C.R.1    Sönnichsen, F.2
  • 33
    • 11844270448 scopus 로고    scopus 로고
    • Aggregation number and critical micellar concentration of surfactant determined by time-dependent static light scattering (TDSLS) and conductivity
    • C. Thévenot, B. Grassl, G. Bastiat, W. Binana, Aggregation number and critical micellar concentration of surfactant determined by time-dependent static light scattering (TDSLS) and conductivity. Colloids Surf. A Physicochem. Eng. Aspects 252, 105-111 (2004).
    • (2004) Colloids Surf. A Physicochem. Eng. Aspects , vol.252 , pp. 105-111
    • Thévenot, C.1    Grassl, B.2    Bastiat, G.3    Binana, W.4
  • 34
    • 70849112486 scopus 로고    scopus 로고
    • Cell signaling in space and time: Where proteins come together and when they're apart
    • J. D. Scott, T. Pawson, Cell signaling in space and time: Where proteins come together and when they're apart. Science 326, 1220-1224 (2009).
    • (2009) Science , vol.326 , pp. 1220-1224
    • Scott, J.D.1    Pawson, T.2
  • 36
    • 53149128421 scopus 로고    scopus 로고
    • Structural and mechanistic insights into STIM1-mediated initiation of store-operated calcium entry
    • P. B. Stathopulos, L. Zheng, G. Y. Li, M. J. Plevin, M. Ikura, Structural and mechanistic insights into STIM1-mediated initiation of store-operated calcium entry. Cell 135, 110-122 (2008).
    • (2008) Cell , vol.135 , pp. 110-122
    • Stathopulos, P.B.1    Zheng, L.2    Li, G.Y.3    Plevin, M.J.4    Ikura, M.5
  • 38
    • 4644340524 scopus 로고    scopus 로고
    • Automated NMR structure calculation with CYANA
    • P. Güntert, Automated NMR structure calculation with CYANA. Methods Mol. Biol. 278, 353-378 (2004).
    • (2004) Methods Mol. Biol. , vol.278 , pp. 353-378
    • Güntert, P.1
  • 39
    • 0036873589 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS
    • T. Herrmann, P. Güntert, K. Wüthrich, Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS. J. Biomol. NMR 24, 171-189 (2002).
    • (2002) J. Biomol. NMR , vol.24 , pp. 171-189
    • Herrmann, T.1    Güntert, P.2    Wüthrich, K.3
  • 42
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • R. A. Laskowski, J. A. Rullmannn, M. W. MacArthur, R. Kaptein, J. M. Thornton, AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8, 477-486 (1996).
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 43
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • R. Koradi, M. Billeter, K. Wüthrich, MOLMOL: A program for display and analysis of macromolecular structures. J. Mol. Graph. 14, 51-55, 29-32 (1996).
    • (1996) J. Mol. Graph. , vol.14
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 44
    • 0032959886 scopus 로고    scopus 로고
    • Identification of constitutive and Ras-inducible phosphorylation sites of KSR: Implications for 14-3-3 binding, mitogen-activated protein kinase binding, and KSR overexpression
    • A. M. Cacace, N. R. Michaud, M. Therrien, K. Mathes, T. Copeland, G. M. Rubin, D. K. Morrison, Identification of constitutive and Ras-inducible phosphorylation sites of KSR: Implications for 14-3-3 binding, mitogen-activated protein kinase binding, and KSR overexpression. Mol. Cell. Biol. 19, 229-240 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 229-240
    • Cacace, A.M.1    Michaud, N.R.2    Therrien, M.3    Mathes, K.4    Copeland, T.5    Rubin, G.M.6    Morrison, D.K.7
  • 45
    • 0029850713 scopus 로고    scopus 로고
    • KSR modulates signal propagation within the MAPK cascade
    • M. Therrien, N. R. Michaud, G. M. Rubin, D. K. Morrison, KSR modulates signal propagation within the MAPK cascade. Genes Dev. 10, 2684-2695 (1996).
    • (1996) Genes Dev. , vol.10 , pp. 2684-2695
    • Therrien, M.1    Michaud, N.R.2    Rubin, G.M.3    Morrison, D.K.4
  • 46
    • 2942531229 scopus 로고    scopus 로고
    • The molecular scaffold KSR1 regulates the proliferative and oncogenic potential of cells
    • R. L. Kortum, R. E. Lewis, The molecular scaffold KSR1 regulates the proliferative and oncogenic potential of cells. Mol. Cell. Biol. 24, 4407-4416 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4407-4416
    • Kortum, R.L.1    Lewis, R.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.