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Volumn 426, Issue 15, 2014, Pages 2755-2768

Molecular conformation of the full-length tumor suppressor NF2/merlin - A small-angle neutron scattering study

Author keywords

Ezrin; Merlin; neurofibromatosis type 2; phosphatidylinositol 4,5 bisphosphate; small angle neutron scattering

Indexed keywords

MERLIN; MERLIN(S518D) PROTEIN; MUTANT PROTEIN; NHERF1 PROTEIN; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; PROTEIN; UNCLASSIFIED DRUG; EZRIN; MOESIN;

EID: 84904268344     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2014.05.011     Document Type: Article
Times cited : (20)

References (66)
  • 1
    • 78149476036 scopus 로고    scopus 로고
    • The NF2 tumor suppressor, Merlin, regulates epidermal development through the establishment of a junctional polarity complex
    • A.B. Gladden, A.M. Hebert, E.E. Schneeberger, and A.I. McClatchey The NF2 tumor suppressor, Merlin, regulates epidermal development through the establishment of a junctional polarity complex Dev Cell 19 2010 727 739
    • (2010) Dev Cell , vol.19 , pp. 727-739
    • Gladden, A.B.1    Hebert, A.M.2    Schneeberger, E.E.3    McClatchey, A.I.4
  • 2
    • 0027405720 scopus 로고
    • A novel moesin-, ezrin-, radixin-like gene is a candidate for the neurofibromatosis 2 tumor suppressor
    • J.A. Trofatter, M.M. MacCollin, J.L. Rutter, J.R. Murrell, M.P. Duyao, and D.M. Parry et al. A novel moesin-, ezrin-, radixin-like gene is a candidate for the neurofibromatosis 2 tumor suppressor Cell 72 1993 791 800
    • (1993) Cell , vol.72 , pp. 791-800
    • Trofatter, J.A.1    Maccollin, M.M.2    Rutter, J.L.3    Murrell, J.R.4    Duyao, M.P.5    Parry, D.M.6
  • 3
    • 0028928346 scopus 로고
    • Expression of the neurofibromatosis 2 (NF2) gene isoforms during rat embryonic development
    • D.H. Gutmann, D.E. Wright, R.T. Geist, and W.D. Snider Expression of the neurofibromatosis 2 (NF2) gene isoforms during rat embryonic development Hum Mol Genet 4 1995 471 478
    • (1995) Hum Mol Genet , vol.4 , pp. 471-478
    • Gutmann, D.H.1    Wright, D.E.2    Geist, R.T.3    Snider, W.D.4
  • 4
    • 0030924657 scopus 로고    scopus 로고
    • The Nf2 tumor suppressor gene product is essential for extraembryonic development immediately prior to gastrulation
    • A.I. McClatchey, I. Saotome, V. Ramesh, J.F. Gusella, and T. Jacks The Nf2 tumor suppressor gene product is essential for extraembryonic development immediately prior to gastrulation Genes Dev 11 1997 1253 1265
    • (1997) Genes Dev , vol.11 , pp. 1253-1265
    • McClatchey, A.I.1    Saotome, I.2    Ramesh, V.3    Gusella, J.F.4    Jacks, T.5
  • 5
    • 85027926960 scopus 로고    scopus 로고
    • Merlin: A tumour suppressor with functions at the cell cortex and in the nucleus
    • W. Li, J. Cooper, M.A. Karajannis, and F.G. Giancotti Merlin: a tumour suppressor with functions at the cell cortex and in the nucleus EMBO Rep 13 2012 204 215
    • (2012) EMBO Rep , vol.13 , pp. 204-215
    • Li, W.1    Cooper, J.2    Karajannis, M.A.3    Giancotti, F.G.4
  • 6
    • 60149106862 scopus 로고    scopus 로고
    • Merlin regulates transmembrane receptor accumulation and signaling at the plasma membrane in primary mouse Schwann cells and in human schwannomas
    • D. Lallemand, J. Manent, A. Couvelard, A. Watilliaux, M. Siena, and F. Chareyre et al. Merlin regulates transmembrane receptor accumulation and signaling at the plasma membrane in primary mouse Schwann cells and in human schwannomas Oncogene 28 2008 854 865
    • (2008) Oncogene , vol.28 , pp. 854-865
    • Lallemand, D.1    Manent, J.2    Couvelard, A.3    Watilliaux, A.4    Siena, M.5    Chareyre, F.6
  • 7
    • 0035871299 scopus 로고    scopus 로고
    • The NF2 tumor suppressor gene product, merlin, mediates contact inhibition of growth through interactions with CD44
    • H. Morrison, L.S. Sherman, J. Legg, F. Banine, C. Isacke, and C.A. Haipek et al. The NF2 tumor suppressor gene product, merlin, mediates contact inhibition of growth through interactions with CD44 Genes Dev 15 2001 968 980
    • (2001) Genes Dev , vol.15 , pp. 968-980
    • Morrison, H.1    Sherman, L.S.2    Legg, J.3    Banine, F.4    Isacke, C.5    Haipek, C.A.6
  • 8
    • 27544514090 scopus 로고    scopus 로고
    • Merlin/NF-2 mediates contact inhibition of growth by suppressing recruitment of Rac to the plasma membrane
    • T. Okada, M. Lopez-Lago, and F.G. Giancotti Merlin/NF-2 mediates contact inhibition of growth by suppressing recruitment of Rac to the plasma membrane J Cell Biol 171 2005 361 371
    • (2005) J Cell Biol , vol.171 , pp. 361-371
    • Okada, T.1    Lopez-Lago, M.2    Giancotti, F.G.3
  • 9
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: The next generation
    • D. Hanahan, and Robert A. Weinberg Hallmarks of cancer: the next generation Cell 144 2011 646 674
    • (2011) Cell , vol.144 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 10
    • 79953753962 scopus 로고    scopus 로고
    • A tight junction-associated Merlin-angiomotin complex mediates Merlin's regulation of mitogenic signaling and tumor suppressive functions
    • C. Yi, S. Troutman, D. Fera, A. Stemmer-Rachamimov, J.L. Avila, and N. Christian et al. A tight junction-associated Merlin-angiomotin complex mediates Merlin's regulation of mitogenic signaling and tumor suppressive functions Cancer Cell 19 2011 527 540
    • (2011) Cancer Cell , vol.19 , pp. 527-540
    • Yi, C.1    Troutman, S.2    Fera, D.3    Stemmer-Rachamimov, A.4    Avila, J.L.5    Christian, N.6
  • 12
    • 38949104753 scopus 로고    scopus 로고
    • Localization to the cortical cytoskeleton is necessary for Nf2/merlin-dependent epidermal growth factor receptor silencing
    • B.K. Cole, M. Curto, A.W. Chan, and A.I. McClatchey Localization to the cortical cytoskeleton is necessary for Nf2/merlin-dependent epidermal growth factor receptor silencing Mol Cell Biol 28 2008 1274 1284
    • (2008) Mol Cell Biol , vol.28 , pp. 1274-1284
    • Cole, B.K.1    Curto, M.2    Chan, A.W.3    McClatchey, A.I.4
  • 13
    • 76749108011 scopus 로고    scopus 로고
    • Merlin/NF2 suppresses tumorigenesis by inhibiting the E3 ubiquitin ligase CRL4(DCAF1) in the nucleus
    • W. Li, L. You, J. Cooper, G. Schiavon, A. Pepe-Caprio, and L. Zhou et al. Merlin/NF2 suppresses tumorigenesis by inhibiting the E3 ubiquitin ligase CRL4(DCAF1) in the nucleus Cell 140 2010 477 490
    • (2010) Cell , vol.140 , pp. 477-490
    • Li, W.1    You, L.2    Cooper, J.3    Schiavon, G.4    Pepe-Caprio, A.5    Zhou, L.6
  • 14
    • 18044399847 scopus 로고    scopus 로고
    • The Nf2 tumor suppressor, merlin, functions in Rac-dependent signaling
    • R.J. Shaw, J.G. Paez, M. Curto, A. Yaktine, W.M. Pruitt, and I. Saotome et al. The Nf2 tumor suppressor, merlin, functions in Rac-dependent signaling Dev Cell 1 2001 63 72
    • (2001) Dev Cell , vol.1 , pp. 63-72
    • Shaw, R.J.1    Paez, J.G.2    Curto, M.3    Yaktine, A.4    Pruitt, W.M.5    Saotome, I.6
  • 15
    • 34848921532 scopus 로고    scopus 로고
    • Akt phosphorylation regulates the tumour-suppressor merlin through ubiquitination and degradation
    • X. Tang, S.W. Jang, X. Wang, Z. Liu, S.M. Bahr, and S.Y. Sun et al. Akt phosphorylation regulates the tumour-suppressor merlin through ubiquitination and degradation Nat Cell Biol 9 2007 1199 1207
    • (2007) Nat Cell Biol , vol.9 , pp. 1199-1207
    • Tang, X.1    Jang, S.W.2    Wang, X.3    Liu, Z.4    Bahr, S.M.5    Sun, S.Y.6
  • 16
    • 0037155916 scopus 로고    scopus 로고
    • Merlin phosphorylation by p21-activated kinase 2 and effects of phosphorylation on Merlin localization
    • J.L. Kissil, K.C. Johnson, M.S. Eckman, and T. Jacks Merlin phosphorylation by p21-activated kinase 2 and effects of phosphorylation on Merlin localization J Biol Chem 277 2002 10394 10399
    • (2002) J Biol Chem , vol.277 , pp. 10394-10399
    • Kissil, J.L.1    Johnson, K.C.2    Eckman, M.S.3    Jacks, T.4
  • 17
    • 0037059807 scopus 로고    scopus 로고
    • P21-activated kinase links Rac/Cdc42 signaling to merlin
    • G.H. Xiao, A. Beeser, J. Chernoff, and J.R. Testa p21-activated kinase links Rac/Cdc42 signaling to merlin J Biol Chem 277 2002 883 886
    • (2002) J Biol Chem , vol.277 , pp. 883-886
    • Xiao, G.H.1    Beeser, A.2    Chernoff, J.3    Testa, J.R.4
  • 18
    • 0842329800 scopus 로고    scopus 로고
    • Effect of merlin phosphorylation on neurofibromatosis 2 (NF2) gene function
    • E.I. Surace, C.A. Haipek, and D.H. Gutmann Effect of merlin phosphorylation on neurofibromatosis 2 (NF2) gene function Oncogene 23 2004 580 587
    • (2004) Oncogene , vol.23 , pp. 580-587
    • Surace, E.I.1    Haipek, C.A.2    Gutmann, D.H.3
  • 19
    • 33746722720 scopus 로고    scopus 로고
    • Tumorigenic transformation by CPI-17 through inhibition of a merlin phosphatase
    • H. Jin, T. Sperka, P. Herrlich, and H. Morrison Tumorigenic transformation by CPI-17 through inhibition of a merlin phosphatase Nature 442 2006 576 579
    • (2006) Nature , vol.442 , pp. 576-579
    • Jin, H.1    Sperka, T.2    Herrlich, P.3    Morrison, H.4
  • 21
    • 0029121577 scopus 로고
    • Ezrin self-association involves binding of an N-terminal domain to a normally masked C-terminal domain that includes the F-actin binding site
    • R. Gary, and A. Bretscher Ezrin self-association involves binding of an N-terminal domain to a normally masked C-terminal domain that includes the F-actin binding site Mol Biol Cell 6 1995 1061 1075
    • (1995) Mol Biol Cell , vol.6 , pp. 1061-1075
    • Gary, R.1    Bretscher, A.2
  • 22
    • 33846100727 scopus 로고    scopus 로고
    • Self-masking in an intact ERM-merlin protein: An active role for the central alpha-helical domain
    • Q. Li, M.R. Nance, R. Kulikauskas, K. Nyberg, R. Fehon, and P.A. Karplus et al. Self-masking in an intact ERM-merlin protein: an active role for the central alpha-helical domain J Mol Biol 365 2007 1446 1459
    • (2007) J Mol Biol , vol.365 , pp. 1446-1459
    • Li, Q.1    Nance, M.R.2    Kulikauskas, R.3    Nyberg, K.4    Fehon, R.5    Karplus, P.A.6
  • 23
    • 1442285361 scopus 로고    scopus 로고
    • Phosphoinositide binding and phosphorylation act sequentially in the activation mechanism of ezrin
    • B.T. Fievet, A. Gautreau, C. Roy, L. Del Maestro, P. Mangeat, and D. Louvard et al. Phosphoinositide binding and phosphorylation act sequentially in the activation mechanism of ezrin J Cell Biol 164 2004 653 659
    • (2004) J Cell Biol , vol.164 , pp. 653-659
    • Fievet, B.T.1    Gautreau, A.2    Roy, C.3    Del Maestro, L.4    Mangeat, P.5    Louvard, D.6
  • 24
    • 0030835761 scopus 로고    scopus 로고
    • A dual involvement of the amino-terminal domain of ezrin in F- and G-actin binding
    • C. Roy, M. Martin, and P. Mangeat A dual involvement of the amino-terminal domain of ezrin in F- and G-actin binding J Biol Chem 272 1997 20088 20095
    • (1997) J Biol Chem , vol.272 , pp. 20088-20095
    • Roy, C.1    Martin, M.2    Mangeat, P.3
  • 25
    • 0029862987 scopus 로고    scopus 로고
    • Biochemical characterization of ezrin-actin interaction
    • X. Yao, L. Cheng, and J.G. Forte Biochemical characterization of ezrin-actin interaction J Biol Chem 271 1996 7224 7229
    • (1996) J Biol Chem , vol.271 , pp. 7224-7229
    • Yao, X.1    Cheng, L.2    Forte, J.G.3
  • 26
    • 0033607687 scopus 로고    scopus 로고
    • Interdomain interaction of Merlin isoforms and its influence on intermolecular binding to NHE-RF
    • C. Gonzalez-Agosti, T. Wiederhold, M.E. Herndon, J. Gusella, and V. Ramesh Interdomain interaction of Merlin isoforms and its influence on intermolecular binding to NHE-RF J Biol Chem 274 1999 34438 34442
    • (1999) J Biol Chem , vol.274 , pp. 34438-34442
    • Gonzalez-Agosti, C.1    Wiederhold, T.2    Herndon, M.E.3    Gusella, J.4    Ramesh, V.5
  • 27
    • 0035831501 scopus 로고    scopus 로고
    • Hierarchy of Merlin and Ezrin N- and C-terminal domain interactions in homo- and heterotypic associations and their relationship to binding of scaffolding proteins EBP50 and E3KARP
    • R. Nguyen, D. Reczek, and A. Bretscher Hierarchy of Merlin and Ezrin N- and C-terminal domain interactions in homo- and heterotypic associations and their relationship to binding of scaffolding proteins EBP50 and E3KARP J Biol Chem 276 2001 7621 7629
    • (2001) J Biol Chem , vol.276 , pp. 7621-7629
    • Nguyen, R.1    Reczek, D.2    Bretscher, A.3
  • 28
    • 0030775695 scopus 로고    scopus 로고
    • Interdomain binding mediates tumor growth suppression by the NF2 gene product
    • L. Sherman, H.M. Xu, R.T. Geist, S. Saporito-Irwin, N. Howells, and H. Ponta et al. Interdomain binding mediates tumor growth suppression by the NF2 gene product Oncogene 15 1997 2505 2509
    • (1997) Oncogene , vol.15 , pp. 2505-2509
    • Sherman, L.1    Xu, H.M.2    Geist, R.T.3    Saporito-Irwin, S.4    Howells, N.5    Ponta, H.6
  • 29
    • 9144234897 scopus 로고    scopus 로고
    • Serine 518 phosphorylation modulates merlin intramolecular association and binding to critical effectors important for NF2 growth suppression
    • R. Rong, E.I. Surace, C.A. Haipek, D.H. Gutmann, and K. Ye Serine 518 phosphorylation modulates merlin intramolecular association and binding to critical effectors important for NF2 growth suppression Oncogene 23 2004 8447 8454
    • (2004) Oncogene , vol.23 , pp. 8447-8454
    • Rong, R.1    Surace, E.I.2    Haipek, C.A.3    Gutmann, D.H.4    Ye, K.5
  • 31
    • 84859856596 scopus 로고    scopus 로고
    • The tumor suppressor merlin controls growth in its open state, and phosphorylation converts it to a less-active more-closed state
    • I. Sher, C.O. Hanemann, P.A. Karplus, and A. Bretscher The tumor suppressor merlin controls growth in its open state, and phosphorylation converts it to a less-active more-closed state Dev Cell 22 2012 703 705
    • (2012) Dev Cell , vol.22 , pp. 703-705
    • Sher, I.1    Hanemann, C.O.2    Karplus, P.A.3    Bretscher, A.4
  • 32
    • 84868262769 scopus 로고    scopus 로고
    • Open conformation of Ezrin bound to phosphatidylinositol 4,5-bisphosphate and to F-actin revealed by neutron scattering
    • J.J. Jayasundar, J.H. Ju, L. He, D. Liu, F. Meilleur, and J. Zhao et al. Open conformation of Ezrin bound to phosphatidylinositol 4,5-bisphosphate and to F-actin revealed by neutron scattering J Biol Chem 287 2012 37119 37133
    • (2012) J Biol Chem , vol.287 , pp. 37119-37133
    • Jayasundar, J.J.1    Ju, J.H.2    He, L.3    Liu, D.4    Meilleur, F.5    Zhao, J.6
  • 33
    • 27844570909 scopus 로고    scopus 로고
    • Ezrin controls the macromolecular complexes formed between an adapter protein Na +/H + exchanger regulatory factor and the cystic fibrosis transmembrane conductance regulator
    • J. Li, Z. Dai, D. Jana, D.J. Callaway, and Z. Bu Ezrin controls the macromolecular complexes formed between an adapter protein Na +/H + exchanger regulatory factor and the cystic fibrosis transmembrane conductance regulator J Biol Chem 280 2005 37634 37643
    • (2005) J Biol Chem , vol.280 , pp. 37634-37643
    • Li, J.1    Dai, Z.2    Jana, D.3    Callaway, D.J.4    Bu, Z.5
  • 34
    • 0030608877 scopus 로고    scopus 로고
    • Identification of EBP50: A PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family
    • D. Reczek, M. Berryman, and A. Bretscher Identification of EBP50: a PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family J Cell Biol 139 1997 169 179
    • (1997) J Cell Biol , vol.139 , pp. 169-179
    • Reczek, D.1    Berryman, M.2    Bretscher, A.3
  • 35
    • 33645992471 scopus 로고    scopus 로고
    • Structural basis for NHERF recognition by ERM proteins
    • S. Terawaki, R. Maesaki, and T. Hakoshima Structural basis for NHERF recognition by ERM proteins Structure 14 2006 777 789
    • (2006) Structure , vol.14 , pp. 777-789
    • Terawaki, S.1    Maesaki, R.2    Hakoshima, T.3
  • 36
    • 2342436207 scopus 로고    scopus 로고
    • The EBP50-moesin interaction involves a binding site regulated by direct masking on the FERM domain
    • C.M. Finnerty, D. Chambers, J. Ingraffea, H.R. Faber, P.A. Karplus, and A. Bretscher The EBP50-moesin interaction involves a binding site regulated by direct masking on the FERM domain J Cell Sci 117 2004 1547 1552
    • (2004) J Cell Sci , vol.117 , pp. 1547-1552
    • Finnerty, C.M.1    Chambers, D.2    Ingraffea, J.3    Faber, H.R.4    Karplus, P.A.5    Bretscher, A.6
  • 37
    • 68949167656 scopus 로고    scopus 로고
    • Ezrin induces long-range interdomain allostery in the scaffolding protein NHERF1
    • J. Li, D.J. Callaway, and Z. Bu Ezrin induces long-range interdomain allostery in the scaffolding protein NHERF1 J Mol Biol 392 2009 166 180
    • (2009) J Mol Biol , vol.392 , pp. 166-180
    • Li, J.1    Callaway, D.J.2    Bu, Z.3
  • 38
    • 0034724536 scopus 로고    scopus 로고
    • Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain
    • M.A. Pearson, D. Reczek, A. Bretscher, and P.A. Karplus Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain Cell 101 2000 259 270
    • (2000) Cell , vol.101 , pp. 259-270
    • Pearson, M.A.1    Reczek, D.2    Bretscher, A.3    Karplus, P.A.4
  • 39
    • 0031890998 scopus 로고    scopus 로고
    • NHE-RF, a regulatory cofactor for Na(+)-H(+) exchange, is a common interactor for merlin and ERM (MERM) proteins
    • A. Murthy, C. Gonzalez-Agosti, E. Cordero, D. Pinney, C. Candia, and F. Solomon et al. NHE-RF, a regulatory cofactor for Na(+)-H(+) exchange, is a common interactor for merlin and ERM (MERM) proteins J Biol Chem 273 1998 1273 1276
    • (1998) J Biol Chem , vol.273 , pp. 1273-1276
    • Murthy, A.1    Gonzalez-Agosti, C.2    Cordero, E.3    Pinney, D.4    Candia, C.5    Solomon, F.6
  • 40
    • 34848850791 scopus 로고    scopus 로고
    • Protein kinase C phosphorylation disrupts Na +/H + exchanger regulatory factor 1 autoinhibition and promotes cystic fibrosis transmembrane conductance regulator macromolecular assembly
    • J. Li, P.I. Poulikakos, Z. Dai, J.R. Testa, D.J. Callaway, and Z. Bu Protein kinase C phosphorylation disrupts Na +/H + exchanger regulatory factor 1 autoinhibition and promotes cystic fibrosis transmembrane conductance regulator macromolecular assembly J Biol Chem 282 2007 27086 27099
    • (2007) J Biol Chem , vol.282 , pp. 27086-27099
    • Li, J.1    Poulikakos, P.I.2    Dai, Z.3    Testa, J.R.4    Callaway, D.J.5    Bu, Z.6
  • 41
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • D.I. Svergun Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing Biophys J 76 1999 2879 2886
    • (1999) Biophys J , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 42
    • 34247891557 scopus 로고    scopus 로고
    • Structural characterization of flexible proteins using small-angle X-ray scattering
    • P. Bernado, E. Mylonas, M.V. Petoukhov, M. Blackledge, and D.I. Svergun Structural characterization of flexible proteins using small-angle X-ray scattering J Am Chem Soc 129 2007 5656 5664
    • (2007) J Am Chem Soc , vol.129 , pp. 5656-5664
    • Bernado, P.1    Mylonas, E.2    Petoukhov, M.V.3    Blackledge, M.4    Svergun, D.I.5
  • 43
    • 78049271908 scopus 로고    scopus 로고
    • Phosphatidylinositol 4, 5-bisphosphate-induced conformational change of ezrin and formation of ezrin oligomers
    • K. Carvalho, N. Khalifat, O. Maniti, C. Nicolas, S. Arold, and C. Picart et al. Phosphatidylinositol 4, 5-bisphosphate-induced conformational change of ezrin and formation of ezrin oligomers Biochemistry 49 2010 9318 9327
    • (2010) Biochemistry , vol.49 , pp. 9318-9327
    • Carvalho, K.1    Khalifat, N.2    Maniti, O.3    Nicolas, C.4    Arold, S.5    Picart, C.6
  • 44
    • 84985698663 scopus 로고
    • Determination of molecular weight by neutron scattering
    • B. Jacrot, and G. Zaccai Determination of molecular weight by neutron scattering Biopolymers 20 1981 2413 2426
    • (1981) Biopolymers , vol.20 , pp. 2413-2426
    • Jacrot, B.1    Zaccai, G.2
  • 45
    • 0032805390 scopus 로고    scopus 로고
    • A method for determining transmembrane helix association and orientation in detergent micelles using small angle X-ray scattering
    • Z. Bu, and D.M. Engelman A method for determining transmembrane helix association and orientation in detergent micelles using small angle X-ray scattering Biophys J 77 1999 1064 1073
    • (1999) Biophys J , vol.77 , pp. 1064-1073
    • Bu, Z.1    Engelman, D.M.2
  • 46
    • 4644327724 scopus 로고    scopus 로고
    • Structure-specific DNA-induced conformational changes in Taq polymerase revealed by small angle neutron scattering
    • D.L. Ho, W.M. Byrnes, W.P. Ma, Y. Shi, D.J. Callaway, and Z. Bu Structure-specific DNA-induced conformational changes in Taq polymerase revealed by small angle neutron scattering J Biol Chem 279 2004 39146 39154
    • (2004) J Biol Chem , vol.279 , pp. 39146-39154
    • Ho, D.L.1    Byrnes, W.M.2    Ma, W.P.3    Shi, Y.4    Callaway, D.J.5    Bu, Z.6
  • 47
    • 81755172093 scopus 로고    scopus 로고
    • Unfurling of the band 4.1, ezrin, radixin, moesin (FERM) domain of the merlin tumor suppressor
    • S. Yogesha, A.J. Sharff, M. Giovannini, G. Bricogne, and T. Izard Unfurling of the band 4.1, ezrin, radixin, moesin (FERM) domain of the merlin tumor suppressor Protein Sci 20 2011 2113 2120
    • (2011) Protein Sci , vol.20 , pp. 2113-2120
    • Yogesha, S.1    Sharff, A.J.2    Giovannini, M.3    Bricogne, G.4    Izard, T.5
  • 49
    • 0037155867 scopus 로고    scopus 로고
    • Structural basis for neurofibromatosis type 2: Crystal structure of the merlin FERM domain
    • T. Shimizu, A. Seto, N. Maita, K. Hamada, S. Tsukita, and S. Tsukita et al. Structural basis for neurofibromatosis type 2: crystal structure of the merlin FERM domain J Biol Chem 277 2002 10332 10336
    • (2002) J Biol Chem , vol.277 , pp. 10332-10336
    • Shimizu, T.1    Seto, A.2    Maita, N.3    Hamada, K.4    Tsukita, S.5    Tsukita, S.6
  • 50
    • 84901394649 scopus 로고    scopus 로고
    • Structural basis of the binding of Merlin FERM domain to the E3 ubiquitin ligase substrate adaptor DCAF1
    • Y. Li, Z. Wei, J. Zhang, Z. Yang, and M. Zhang Structural basis of the binding of Merlin FERM domain to the E3 ubiquitin ligase substrate adaptor DCAF1 J Biol Chem 289 2014 14674 14681
    • (2014) J Biol Chem , vol.289 , pp. 14674-14681
    • Li, Y.1    Wei, Z.2    Zhang, J.3    Yang, Z.4    Zhang, M.5
  • 51
    • 78649251653 scopus 로고    scopus 로고
    • Activation of nanoscale allosteric protein domain motion revealed by neutron spin echo spectroscopy
    • B. Farago, J. Li, G. Cornilescu, D.J. Callaway, and Z. Bu Activation of nanoscale allosteric protein domain motion revealed by neutron spin echo spectroscopy Biophys J 99 2010 3473 3482
    • (2010) Biophys J , vol.99 , pp. 3473-3482
    • Farago, B.1    Li, J.2    Cornilescu, G.3    Callaway, D.J.4    Bu, Z.5
  • 52
    • 79956114933 scopus 로고    scopus 로고
    • Proteins MOVE! Protein dynamics and long-range allostery in cell signaling
    • Z. Bu, and D.J. Callaway Proteins MOVE! Protein dynamics and long-range allostery in cell signaling Adv Protein Chem Struct Biol 83 2011 163 221
    • (2011) Adv Protein Chem Struct Biol , vol.83 , pp. 163-221
    • Bu, Z.1    Callaway, D.J.2
  • 53
    • 29144461924 scopus 로고    scopus 로고
    • Coupled protein domain motion in Taq polymerase revealed by neutron spin-echo spectroscopy
    • Z. Bu, R. Biehl, M. Monkenbusch, D. Richter, and D.J. Callaway Coupled protein domain motion in Taq polymerase revealed by neutron spin-echo spectroscopy Proc Natl Acad Sci U S A 102 2005 17646 17651
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 17646-17651
    • Bu, Z.1    Biehl, R.2    Monkenbusch, M.3    Richter, D.4    Callaway, D.J.5
  • 56
    • 1942519695 scopus 로고    scopus 로고
    • Electrostatic sequestration of PIP2 on phospholipid membranes by basic/aromatic regions of proteins
    • A. Gambhir, G. Hangyas-Mihalyne, I. Zaitseva, D.S. Cafiso, J. Wang, and D. Murray et al. Electrostatic sequestration of PIP2 on phospholipid membranes by basic/aromatic regions of proteins Biophys J 86 2004 2188 2207
    • (2004) Biophys J , vol.86 , pp. 2188-2207
    • Gambhir, A.1    Hangyas-Mihalyne, G.2    Zaitseva, I.3    Cafiso, D.S.4    Wang, J.5    Murray, D.6
  • 57
    • 33845313646 scopus 로고    scopus 로고
    • PI(3,4,5)P3 and PI(4,5)P2 lipids target proteins with polybasic clusters to the plasma membrane
    • W.D. Heo, T. Inoue, W.S. Park, M.L. Kim, B.O. Park, and T.J. Wandless et al. PI(3,4,5)P3 and PI(4,5)P2 lipids target proteins with polybasic clusters to the plasma membrane Science 314 2006 1458 1461
    • (2006) Science , vol.314 , pp. 1458-1461
    • Heo, W.D.1    Inoue, T.2    Park, W.S.3    Kim, M.L.4    Park, B.O.5    Wandless, T.J.6
  • 58
    • 79956093702 scopus 로고    scopus 로고
    • FERM domain phosphoinositide binding targets merlin to the membrane and is essential for its growth-suppressive function
    • T. Mani, R.F. Hennigan, L.A. Foster, D.G. Conrady, A.B. Herr, and W. Ip FERM domain phosphoinositide binding targets merlin to the membrane and is essential for its growth-suppressive function Mol Cell Biol 31 2011 1983 1996
    • (2011) Mol Cell Biol , vol.31 , pp. 1983-1996
    • Mani, T.1    Hennigan, R.F.2    Foster, L.A.3    Conrady, D.G.4    Herr, A.B.5    Ip, W.6
  • 59
    • 0034722326 scopus 로고    scopus 로고
    • Mutagenesis of the phosphatidylinositol 4,5-bisphosphate (PIP2) binding site in the Nh2-terminal domain of Ezrin correlates with its altered cellular distribution
    • C. Barret, C. Roy, P. Montcourrier, P. Mangeat, and V. Niggli Mutagenesis of the phosphatidylinositol 4,5-bisphosphate (PIP2) binding site in the Nh2-terminal domain of Ezrin correlates with its altered cellular distribution J Cell Biol 151 2000 1067 1080
    • (2000) J Cell Biol , vol.151 , pp. 1067-1080
    • Barret, C.1    Roy, C.2    Montcourrier, P.3    Mangeat, P.4    Niggli, V.5
  • 60
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • L. Whitmore, and B.A. Wallace DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data Nucleic Acids Res 32 2004 W668 W673
    • (2004) Nucleic Acids Res , vol.32
    • Whitmore, L.1    Wallace, B.A.2
  • 61
    • 77957368818 scopus 로고    scopus 로고
    • The extended Q-range small-angle neutron scattering diffractometer at the SNS
    • J.K. Zhao, C.Y. Gao, and D. Liu The extended Q-range small-angle neutron scattering diffractometer at the SNS J Appl Crystallogr 43 2010 1068 1077
    • (2010) J Appl Crystallogr , vol.43 , pp. 1068-1077
    • Zhao, J.K.1    Gao, C.Y.2    Liu, D.3
  • 62
    • 85055706702 scopus 로고
    • Absolute calibration of small-angle neutron-scattering data
    • G.D. Wignall, and F.S. Bates Absolute calibration of small-angle neutron-scattering data J Appl Crystallogr 20 1987 28 40
    • (1987) J Appl Crystallogr , vol.20 , pp. 28-40
    • Wignall, G.D.1    Bates, F.S.2
  • 63
    • 0026244044 scopus 로고
    • GNOM - A program package for small-angle scattering data-processing
    • A.V. Semenyuk, and D.I. Svergun GNOM - a program package for small-angle scattering data-processing J Appl Crystallogr 24 1991 537 540
    • (1991) J Appl Crystallogr , vol.24 , pp. 537-540
    • Semenyuk, A.V.1    Svergun, D.I.2
  • 64
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • V.V. Volkov, and D.I. Svergun Uniqueness of ab initio shape determination in small-angle scattering J Appl Crystallogr 36 2003 860 864
    • (2003) J Appl Crystallogr , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 65
    • 0035209087 scopus 로고    scopus 로고
    • Using Situs for the registration of protein structures with low-resolution bead models from X-ray solution scattering
    • W. Wriggers, and P. Chacón Using Situs for the registration of protein structures with low-resolution bead models from X-ray solution scattering J Appl Crystallogr 34 2001 773 776
    • (2001) J Appl Crystallogr , vol.34 , pp. 773-776
    • Wriggers, W.1    Chacón, P.2


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