메뉴 건너뛰기




Volumn 105, Issue 33, 2008, Pages 11748-11753

Modulation of actin structure and function by phosphorylation of Tyr-53 and profilin binding

Author keywords

Actin phosphorylation; Dictyostelium discoideum actin; Gelsolin actin structure; Profilin actin structure; pY53 actin structure

Indexed keywords

ALPHA ACTIN; BETA ACTIN; DEOXYRIBONUCLEASE I; GELSOLIN; PROFILIN; SUBTILISIN; TYROSINE;

EID: 50149116323     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0805852105     Document Type: Article
Times cited : (51)

References (44)
  • 1
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard TD, Borisy GG (2003) Cellular motility driven by assembly and disassembly of actin filaments. Cell 112:453-465.
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 4
    • 21144458164 scopus 로고    scopus 로고
    • Immunoaffinity profiling of tyrosine phosphorylation in cancer cells
    • Rush J, et al. (2005) Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol 23:94-101.
    • (2005) Nat Biotechnol , vol.23 , pp. 94-101
    • Rush, J.1
  • 5
    • 0342918649 scopus 로고    scopus 로고
    • Tyrosine phosphorylation in plant bending
    • Kameyama K, et al. (2000) Tyrosine phosphorylation in plant bending. Nature 407:37.
    • (2000) Nature , vol.407 , pp. 37
    • Kameyama, K.1
  • 6
    • 0026636932 scopus 로고
    • Stage-specific tyrosine phosphorylation of actin in Dictyostelium discoideum cells
    • Schweiger A, Mihalache O, Ecke M, Gerisch G (1992) Stage-specific tyrosine phosphorylation of actin in Dictyostelium discoideum cells. J Cell Sci 102:601-609.
    • (1992) J Cell Sci , vol.102 , pp. 601-609
    • Schweiger, A.1    Mihalache, O.2    Ecke, M.3    Gerisch, G.4
  • 7
    • 0027397026 scopus 로고
    • Tyrosine phosphorylation of actin in Dictyostelium associated with cell-shape changes
    • Howard PK, Sefton BM, Firtel RA (1993) Tyrosine phosphorylation of actin in Dictyostelium associated with cell-shape changes. Science 259:241-244.
    • (1993) Science , vol.259 , pp. 241-244
    • Howard, P.K.1    Sefton, B.M.2    Firtel, R.A.3
  • 8
    • 0028803976 scopus 로고
    • Stress-induced tyrosine phosphorylation of actin in Dictyostelium cells and localization of the phosphorylation site to tyrosine-53 adjacent to the DNase I binding loop
    • Jungbluth A, et al. (1995) Stress-induced tyrosine phosphorylation of actin in Dictyostelium cells and localization of the phosphorylation site to tyrosine-53 adjacent to the DNase I binding loop. FEBS Lett 375:87-90.
    • (1995) FEBS Lett , vol.375 , pp. 87-90
    • Jungbluth, A.1
  • 9
    • 0030893487 scopus 로고    scopus 로고
    • Endogenous autoinhibitors regulate changes in actin tyrosine phosphorylation during Dictyostelium spore germination
    • Gauthier ML, Lydan MA, O'Day D, Cotter AD (1997) Endogenous autoinhibitors regulate changes in actin tyrosine phosphorylation during Dictyostelium spore germination. Cell Signal 9:79-83.
    • (1997) Cell Signal , vol.9 , pp. 79-83
    • Gauthier, M.L.1    Lydan, M.A.2    O'Day, D.3    Cotter, A.D.4
  • 10
    • 0031729828 scopus 로고    scopus 로고
    • High levels of actin tyrosine phosphorylation: Correlation with the dormant state of Dictyostelium spores
    • Kishi Y, Clements C, Mahadeo DC, Cotter DA, Sameshima M (1998) High levels of actin tyrosine phosphorylation: Correlation with the dormant state of Dictyostelium spores. J Cell Sci 111:2923-2932.
    • (1998) J Cell Sci , vol.111 , pp. 2923-2932
    • Kishi, Y.1    Clements, C.2    Mahadeo, D.C.3    Cotter, D.A.4    Sameshima, M.5
  • 11
    • 33748796662 scopus 로고    scopus 로고
    • Phosphorylation of actin Tyr-53 inhibits filament nucleation and elongation and destabilizes filaments
    • Liu X, Shu S, Hong MS, Levine RL, Korn ED (2006) Phosphorylation of actin Tyr-53 inhibits filament nucleation and elongation and destabilizes filaments. Proc Natl Acad Sci USA 103:13694-13699.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 13694-13699
    • Liu, X.1    Shu, S.2    Hong, M.S.3    Levine, R.L.4    Korn, E.D.5
  • 12
    • 0346103752 scopus 로고    scopus 로고
    • Cell polarity and Dictyostelium development
    • Williams HP, Harwood AJ (2003) Cell polarity and Dictyostelium development. Curr Opin Microbiol 6:621-627.
    • (2003) Curr Opin Microbiol , vol.6 , pp. 621-627
    • Williams, H.P.1    Harwood, A.J.2
  • 13
    • 0027983090 scopus 로고
    • Strong increase in the tyrosine phosphorylation of actin upon inhibition of oxidative phosphorylation: Correlation with reversible rearrangements in the actin skeleton of Dictyostelium cells
    • Jungbluth A, et al. (1994) Strong increase in the tyrosine phosphorylation of actin upon inhibition of oxidative phosphorylation: correlation with reversible rearrangements in the actin skeleton of Dictyostelium cells. J Cell Sci 107:117-125.
    • (1994) J Cell Sci , vol.107 , pp. 117-125
    • Jungbluth, A.1
  • 15
    • 0032558990 scopus 로고    scopus 로고
    • Intrastrand cross-linked actin between Gln-41 and Cys-374. I. Mapping of sites cross-linked in F-actin by N-(4-azido-2-nitrophenyl) putrescine
    • Hegyi G, et al. (1998) Intrastrand cross-linked actin between Gln-41 and Cys-374. I. Mapping of sites cross-linked in F-actin by N-(4-azido-2-nitrophenyl) putrescine. Biochemistry 37:17784-17792.
    • (1998) Biochemistry , vol.37 , pp. 17784-17792
    • Hegyi, G.1
  • 16
    • 0036213647 scopus 로고    scopus 로고
    • Role of the DNase-I-binding loop in dynamic properties of actin filament
    • Khaitlina SY, Strzelecka-Golaszewska H (2002) Role of the DNase-I-binding loop in dynamic properties of actin filament. Biophys J 82:321-334.
    • (2002) Biophys J , vol.82 , pp. 321-334
    • Khaitlina, S.Y.1    Strzelecka-Golaszewska, H.2
  • 18
    • 0019194944 scopus 로고
    • Acanthamoeba profilin interacts with G-actin to increase the rate of exchange of actin-bound adenosine 5′-triphosphate
    • Mockrin SC, Korn ED (1980) Acanthamoeba profilin interacts with G-actin to increase the rate of exchange of actin-bound adenosine 5′-triphosphate. Biochemistry 19:5359-5362.
    • (1980) Biochemistry , vol.19 , pp. 5359-5362
    • Mockrin, S.C.1    Korn, E.D.2
  • 21
    • 35649021883 scopus 로고    scopus 로고
    • Structural basis for the recruitment of profilin-actin complexes during filament elongation by Ena/VASP
    • Ferron F, Rebowski G, Lee SH, Dominguez R (2007) Structural basis for the recruitment of profilin-actin complexes during filament elongation by Ena/VASP. EMBO J 26:4597-4606.
    • (2007) EMBO J , vol.26 , pp. 4597-4606
    • Ferron, F.1    Rebowski, G.2    Lee, S.H.3    Dominguez, R.4
  • 23
    • 0027251071 scopus 로고
    • Structure of gelsolin segment 1-actin complex and the mechanism of filament severing
    • McLaughlin PJ, Gooch JT, Mannherz HG, Weeds AG (1993) Structure of gelsolin segment 1-actin complex and the mechanism of filament severing. Nature 364:685-692.
    • (1993) Nature , vol.364 , pp. 685-692
    • McLaughlin, P.J.1    Gooch, J.T.2    Mannherz, H.G.3    Weeds, A.G.4
  • 24
    • 0037062405 scopus 로고    scopus 로고
    • Crystal structures of the vitamin D-binding protein and its complex with actin: Structural basis of the actin-scavenger system
    • Otterbein LR, Cosio C, Graceffa P, Dominguez R (2002) Crystal structures of the vitamin D-binding protein and its complex with actin: Structural basis of the actin-scavenger system. Proc Natl Acad Sci USA 99:8003-8008.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 8003-8008
    • Otterbein, L.R.1    Cosio, C.2    Graceffa, P.3    Dominguez, R.4
  • 25
    • 28044470753 scopus 로고    scopus 로고
    • Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly
    • Chereau D, et al. (2005) Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly. Proc Natl Acad Sci USA 102:16644-16649.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 16644-16649
    • Chereau, D.1
  • 26
    • 36048966971 scopus 로고    scopus 로고
    • Toxofilin from Toxoplasma gondii forms a ternary complex with an antiparallel actin dimer
    • Lee SH, Hayes DB, Rebowski G, Tardieux I, Dominguez R (2007) Toxofilin from Toxoplasma gondii forms a ternary complex with an antiparallel actin dimer. Proc Natl Acad Sci USA 104:16122-16127.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 16122-16127
    • Lee, S.H.1    Hayes, D.B.2    Rebowski, G.3    Tardieux, I.4    Dominguez, R.5
  • 27
    • 0345059373 scopus 로고    scopus 로고
    • Trisoxazole macrolide toxins mimic the binding of actin-capping proteins to actin
    • Klenchin VA, et al. (2003) Trisoxazole macrolide toxins mimic the binding of actin-capping proteins to actin. Nat Struct Biol 10:1058-1063.
    • (2003) Nat Struct Biol , vol.10 , pp. 1058-1063
    • Klenchin, V.A.1
  • 28
    • 33846020951 scopus 로고    scopus 로고
    • Crystal structures of expressed non-polymerizable monomeric actin in the ADP and ATP states
    • Rould MA, Wan Q, Joel PB, Lowey S, Trybus KM (2006) Crystal structures of expressed non-polymerizable monomeric actin in the ADP and ATP states. J Biol Chem 281:31909-31919.
    • (2006) J Biol Chem , vol.281 , pp. 31909-31919
    • Rould, M.A.1    Wan, Q.2    Joel, P.B.3    Lowey, S.4    Trybus, K.M.5
  • 29
    • 0035958757 scopus 로고    scopus 로고
    • The crystal structure of uncomplexed actin in the ADP state
    • Otterbein LR, Graceffa P, Dominguez R (2001) The crystal structure of uncomplexed actin in the ADP state. Science 293:708-711.
    • (2001) Science , vol.293 , pp. 708-711
    • Otterbein, L.R.1    Graceffa, P.2    Dominguez, R.3
  • 30
    • 0037610737 scopus 로고    scopus 로고
    • The structure of nonvertebrate actin: Implications for the ATP hydrolytic mechanism
    • Vorobiev S, et al. (2003) The structure of nonvertebrate actin: Implications for the ATP hydrolytic mechanism. Proc Natl Acad Sci USA 100:5760-5765.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 5760-5765
    • Vorobiev, S.1
  • 31
    • 3543012019 scopus 로고    scopus 로고
    • Structure of the N-terminal half of gelsolin bound to actin: Roles in severing, apoptosis and FAF
    • 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.
    • (2004) EMBO J , vol.23 , pp. 2713-2722
    • Burtnick, L.D.1    Urosev, D.2    Irobi, E.3    Narayan, K.4    Robinson, R.C.5
  • 32
    • 0027523454 scopus 로고
    • Localization of the tightly bound divalent-cation-dependent and nucleotide-dependent conformation changes in G-actin using limited proteolytic digestion
    • Strzelecka-Golaszewska H, Moraczewska J, Khaitlina SY, Mossakowska M (1993) Localization of the tightly bound divalent-cation-dependent and nucleotide-dependent conformation changes in G-actin using limited proteolytic digestion. Eur J Biochem 211:731-742.
    • (1993) Eur J Biochem , vol.211 , pp. 731-742
    • Strzelecka-Golaszewska, H.1    Moraczewska, J.2    Khaitlina, S.Y.3    Mossakowska, M.4
  • 33
    • 0029847601 scopus 로고    scopus 로고
    • Effects of the type of divalent cation, Ca2+ or Mg2+, bound at the high-affinity site and of the ionic composition of the solution on the structure of F-actin
    • Strzelecka-Golaszewska H, Wozniak A, Hult T, Lindberg U (1996) Effects of the type of divalent cation, Ca2+ or Mg2+, bound at the high-affinity site and of the ionic composition of the solution on the structure of F-actin. Biochem J 316:713-721.
    • (1996) Biochem J , vol.316 , pp. 713-721
    • Strzelecka-Golaszewska, H.1    Wozniak, A.2    Hult, T.3    Lindberg, U.4
  • 34
    • 4444357229 scopus 로고    scopus 로고
    • Cofilin induced conformational changes in F-actin expose subdomain 2 to proteolysis
    • Muhlrad A, et al. (2004) Cofilin induced conformational changes in F-actin expose subdomain 2 to proteolysis. J Mol Biol 342:1559-1567.
    • (2004) J Mol Biol , vol.342 , pp. 1559-1567
    • Muhlrad, A.1
  • 35
    • 0023894120 scopus 로고
    • Gelsolin has three actin-binding sites
    • Bryan J (1988) Gelsolin has three actin-binding sites. J Cell Biol 106:1553-1562.
    • (1988) J Cell Biol , vol.106 , pp. 1553-1562
    • Bryan, J.1
  • 36
    • 0030575783 scopus 로고    scopus 로고
    • The structure of an open state of beta-actin at 2.65 A resolution
    • Chik JK, Lindberg U, Schutt CE (1996) The structure of an open state of beta-actin at 2.65 A resolution. J Mol Biol 263:607-623.
    • (1996) J Mol Biol , vol.263 , pp. 607-623
    • Chik, J.K.1    Lindberg, U.2    Schutt, C.E.3
  • 37
    • 0035909233 scopus 로고    scopus 로고
    • ATPase activity and conformational changes in the regulation of actin
    • Schuler H (2001) ATPase activity and conformational changes in the regulation of actin. Biochim Biophys Acta 1549:137-147.
    • (2001) Biochim Biophys Acta , vol.1549 , pp. 137-147
    • Schuler, H.1
  • 38
    • 33646189384 scopus 로고    scopus 로고
    • The open nucleotide pocket of the profilin/actin x-ray structure is unstable and closes in the absence of profilin
    • Minehardt TJ, Kollman PA, Cooke R, Pate E (2006) The open nucleotide pocket of the profilin/actin x-ray structure is unstable and closes in the absence of profilin. Biophys J 90:2445-2449.
    • (2006) Biophys J , vol.90 , pp. 2445-2449
    • Minehardt, T.J.1    Kollman, P.A.2    Cooke, R.3    Pate, E.4
  • 39
    • 0027511431 scopus 로고
    • Normal mode analysis of G-actin
    • Tirion MM, ben-Avraham D (1993) Normal mode analysis of G-actin. J Mol Biol 230:186-195.
    • (1993) J Mol Biol , vol.230 , pp. 186-195
    • Tirion, M.M.1    ben-Avraham, D.2
  • 41
    • 0034870406 scopus 로고    scopus 로고
    • Actin allostery again?
    • Egelman EH (2001) Actin allostery again? Nat Struct Biol 8:735-736.
    • (2001) Nat Struct Biol , vol.8 , pp. 735-736
    • Egelman, E.H.1
  • 42
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder H, Sligar SG, Wolynes PG (1991) The energy landscapes and motions of proteins. Science 254:1598-1603.
    • (1991) Science , vol.254 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 43
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • 4
    • CCP4 (1994) The CCP4 suite: Programs for protein crystallography. Acta Crystallogr D 50:760-763.
    • (1994) Acta Crystallogr D , vol.50 , pp. 760-763
    • CCP1
  • 44
    • 0035941045 scopus 로고    scopus 로고
    • Crystal structure of Arp2/3 complex
    • Robinson RC, et al. (2001) Crystal structure of Arp2/3 complex. Science 294:1679-1684.
    • (2001) Science , vol.294 , pp. 1679-1684
    • Robinson, R.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.