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Volumn 106, Issue 33, 2009, Pages 13713-13718

Ca2+ binding by domain 2 plays a critical role in the activation and stabilization of gelsolin

Author keywords

Actin; Calcium activated; Calcium dependent; TIRF

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; GELSOLIN; AMYLOID; CALCIUM; PEPTIDE HYDROLASE;

EID: 69549131224     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0812374106     Document Type: Article
Times cited : (101)

References (30)
  • 2
    • 0021356287 scopus 로고
    • Structure and biosynthesis of cytoplasmic and secreted variants of gelsolin
    • Yin HL, Kwiatkowski DJ, Mole JE, Cole FS (1984) Structure and biosynthesis of cytoplasmic and secreted variants of gelsolin. J Biol Chem 259:5271-5276.
    • (1984) J Biol Chem , vol.259 , pp. 5271-5276
    • Yin, H.L.1    Kwiatkowski, D.J.2    Mole, J.E.3    Cole, F.S.4
  • 3
    • 0023883135 scopus 로고
    • Genomic organization and biosynthesis of secreted and cytoplasmic forms of gelsolin
    • Kwiatkowski DJ, Mehl R, Yin HL (1988) Genomic organization and biosynthesis of secreted and cytoplasmic forms of gelsolin. J Cell Biol 106:375-384. (Pubitemid 18052185)
    • (1988) Journal of Cell Biology , vol.106 , Issue.2 , pp. 375-384
    • Kwiatkowski, D.J.1    Mehl, R.2    Yin, H.L.3
  • 4
    • 0024293322 scopus 로고
    • Nucleotide sequence of pig plasma gelsolin
    • Way M, Weeds A (1988) Nucleotide sequence of pig plasma gelsolin. J Mol Biol 203:1127-1133.
    • (1988) J Mol Biol , vol.203 , pp. 1127-1133
    • Way, M.1    Weeds, A.2
  • 6
    • 0030829385 scopus 로고    scopus 로고
    • The crystal structure of plasma gelsolin: Implications for actin severing, capping, and nucleation
    • Burtnick LD, et al. (1997) The crystal structure of plasma gelsolin: Implications for actin severing, capping, and nucleation. Cell 90:661-670.
    • (1997) Cell , vol.90 , pp. 661-670
    • Burtnick, L.D.1
  • 8
    • 33644954665 scopus 로고    scopus 로고
    • Calcium ion exchange in crystalline gelsolin
    • Chumnarnsilpa S, et al. (2006) Calcium ion exchange in crystalline gelsolin. J Mol Biol 357:773-782.
    • (2006) J Mol Biol , vol.357 , pp. 773-782
    • Chumnarnsilpa, S.1
  • 9
    • 3543012019 scopus 로고    scopus 로고
    • Structure of the N-terminal half of gelsolin bound to actin: Roles in severing, apoptosis and FAF
    • DOI 10.1038/sj.emboj.7600280
    • Burtnick LD, Urosev D, Irobi E, Narayan K, Robinson RC (2004) Structure of the N-terminal half of gelsolin bound to actin: Roles in severing, apoptosis and FAF. EMBO J 23:2713-2722. (Pubitemid 39013544)
    • (2004) EMBO Journal , vol.23 , Issue.14 , pp. 2713-2722
    • Burtnick, L.D.1    Urosev, D.2    Irobi, E.3    Narayan, K.4    Robinson, R.C.5
  • 10
    • 0036171876 scopus 로고    scopus 로고
    • Loss of a metal-binding site in gelsolin leads to familial amyloidosis-Finnish type
    • Kazmirski SL, et al. (2002) Loss of a metal-binding site in gelsolin leads to familial amyloidosis-Finnish type. Nat Struct Biol 9:112-116.
    • (2002) Nat Struct Biol , vol.9 , pp. 112-116
    • Kazmirski, S.L.1
  • 11
    • 0037693763 scopus 로고    scopus 로고
    • Gelsolin domains 4-6 in active, actin-free conformation identifies sites of regulatory calcium ions
    • DOI 10.1016/S0022-2836(03)00383-8
    • Kolappan S, Gooch JT, Weeds AG, McLaughlin PJ (2003) Gelsolin domains 4-6 in active, actin-free conformation identifies sites of regulatory calcium ions. J Mol Biol 329:85-92. (Pubitemid 36555168)
    • (2003) Journal of Molecular Biology , vol.329 , Issue.1 , pp. 85-92
    • Kolappan, S.1    Gooch, J.T.2    Weeds, A.G.3    McLaughlin, P.J.4
  • 14
    • 0028957131 scopus 로고
    • Localization of the calcium-sensitive actin monomer binding site in gelsolin to segment 4 and identification of calcium binding sites
    • Pope BJ, Maciver S, Weeds AG (1995) Localization of the calcium-sensitive actin monomer binding site in gelsolin to segment 4 and identification of calcium binding sites. Biochemistry 34:1583-1588.
    • (1995) Biochemistry , vol.34 , pp. 1583-1588
    • Pope, B.J.1    Maciver, S.2    Weeds, A.G.3
  • 15
    • 0025175562 scopus 로고
    • 2+-induced conformational change of the gelsolin molecule: A dynamic light scattering study
    • 2+-induced conformational change of the gelsolin molecule: A dynamic light scattering study. Biopolymers 30:427-435.
    • (1990) Biopolymers , vol.30 , pp. 427-435
    • Patkowski, A.1    Seils, J.2    Hinssen, H.3    Dorfmuller, T.4
  • 16
    • 0031443215 scopus 로고    scopus 로고
    • Probing the effects of calcium on gelsolin
    • Pope BJ, Gooch JT, Weeds AG (1997) Probing the effects of calcium on gelsolin. Biochemistry 36:15848-15855.
    • (1997) Biochemistry , vol.36 , pp. 15848-15855
    • Pope, B.J.1    Gooch, J.T.2    Weeds, A.G.3
  • 17
    • 34548484574 scopus 로고    scopus 로고
    • 2+ activation of full-length human plasma gelsolin
    • 2+ activation of full-length human plasma gelsolin. J Biol Chem 282:25884-25892.
    • (2007) J Biol Chem , vol.282 , pp. 25884-25892
    • Ashish1
  • 18
    • 0347882733 scopus 로고    scopus 로고
    • Structural analysis of gelsolin using synchrotron protein footprinting
    • Kiselar JG, Janmey PA, Almo SC, Chance MR (2003) Structural analysis of gelsolin using synchrotron protein footprinting. Mol Cell Proteomics 2:1120-1132.
    • (2003) Mol Cell Proteomics , vol.2 , pp. 1120-1132
    • Kiselar, J.G.1    Janmey, P.A.2    Almo, S.C.3    Chance, M.R.4
  • 20
    • 0025779730 scopus 로고
    • Gelsolin-related amyloidosis. Identification of the amyloid protein in Finnish hereditary amyloidosis as a fragment of variant gelsolin
    • Maury CP (1991) Gelsolin-related amyloidosis. Identification of the amyloid protein in Finnish hereditary amyloidosis as a fragment of variant gelsolin. J Clin Invest 87:1195-1199.
    • (1991) J Clin Invest , vol.87 , pp. 1195-1199
    • Maury, C.P.1
  • 21
    • 0035890055 scopus 로고    scopus 로고
    • 2+ stabilization
    • 2+ stabilization. EMBO J 20:6277-6287.
    • (2001) EMBO J , vol.20 , pp. 6277-6287
    • Chen, C.D.1
  • 22
    • 28644437423 scopus 로고    scopus 로고
    • Metalloendoprotease cleavage triggers gelsolin amyloidogenesis
    • Page LJ, et al. (2005) Metalloendoprotease cleavage triggers gelsolin amyloidogenesis. EMBO J 24:4124-4132.
    • (2005) EMBO J , vol.24 , pp. 4124-4132
    • Page, L.J.1
  • 23
    • 0026936594 scopus 로고
    • Gelsolin-derived familial amyloidosis caused by asparagine or tyrosine substitution for aspartic acid at residue 187
    • de la Chapelle A, et al. (1992) Gelsolin-derived familial amyloidosis caused by asparagine or tyrosine substitution for aspartic acid at residue 187. Nat Genet 2:157-160.
    • (1992) Nat Genet , vol.2 , pp. 157-160
    • De La Chapelle, A.1
  • 26
    • 0031015826 scopus 로고    scopus 로고
    • Functional consequences of disulfide bond formation in gelsolin
    • DOI 10.1016/S0014-5793(96)01439-1, PII S0014579396014391
    • Allen PG (1997) Functional consequences of disulfide bond formation in gelsolin. FEBS Lett 401:89-94. (Pubitemid 27051264)
    • (1997) FEBS Letters , vol.401 , Issue.1 , pp. 89-94
    • Allen, P.G.1
  • 28
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276:4866-4871.
    • (1997) Methods Enzymol , vol.276 , pp. 4866-4871
    • Otwinowski, Z.1    Minor, W.2
  • 29
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: Programs for protein crystallography. Acta Crystallograllogr D Biol Crystallogr 50:760-763.
    • (1994) Acta Crystallograllogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 30
    • 18244380348 scopus 로고    scopus 로고
    • High-density miniaturized thermal shift assays as a general strategy for drug discovery
    • Pantoliano MW, et al. (2001) High-density miniaturized thermal shift assays as a general strategy for drug discovery. J Biomol Screen 6:429-440.
    • (2001) J Biomol Screen , vol.6 , pp. 429-440
    • Pantoliano, M.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.