메뉴 건너뛰기




Volumn 106, Issue 50, 2009, Pages 21131-21136

Structural insights into tail-anchored protein binding and membrane insertion by Get3

Author keywords

Asna1 Trc40; ATP binding protein; Crystal structure; Get pathway; Posttranslational targeting

Indexed keywords

ADENOSINE TRIPHOSPHATASE; DIMER; GET3 PROTEIN; MEMBRANE PROTEIN; NUCLEOTIDE; PROTON; UNCLASSIFIED DRUG; ZINC ION;

EID: 75849130606     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0910223106     Document Type: Article
Times cited : (83)

References (50)
  • 1
    • 0029952518 scopus 로고    scopus 로고
    • Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes
    • Rapoport TA, Jungnickel B, Kutay U (1996) Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes. Annu Rev Biochem 65:271-303.
    • (1996) Annu Rev Biochem , vol.65 , pp. 271-303
    • Rapoport, T.A.1    Jungnickel, B.2    Kutay, U.3
  • 5
    • 36749001066 scopus 로고    scopus 로고
    • Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes
    • Rapoport TA (2007) Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes. Nature 450:663-669.
    • (2007) Nature , vol.450 , pp. 663-669
    • Rapoport, T.A.1
  • 6
    • 0028837490 scopus 로고
    • Transport route for synaptobrevin via a novel pathway of insertion into the endoplasmic reticulum membrane
    • Kutay U, Ahnert-Hilger G, Hartmann E, Wiedenmann B, Rapoport TA (1995) Transport route for synaptobrevin via a novel pathway of insertion into the endoplasmic reticulum membrane. EMBO J 14:217-223.
    • (1995) EMBO J , vol.14 , pp. 217-223
    • Kutay, U.1    Ahnert-Hilger, G.2    Hartmann, E.3    Wiedenmann, B.4    Rapoport, T.A.5
  • 7
    • 34547937485 scopus 로고    scopus 로고
    • How tails guide tail-anchored proteins to their destinations
    • Borgese N, Brambillasca S, Colombo S (2007) How tails guide tail-anchored proteins to their destinations. Curr Opin Cell Biol 19:368-375.
    • (2007) Curr Opin Cell Biol , vol.19 , pp. 368-375
    • Borgese, N.1    Brambillasca, S.2    Colombo, S.3
  • 8
    • 34250183921 scopus 로고    scopus 로고
    • Post-translational integration of tail-anchored proteins is facilitated by defined molecular chaperones
    • Abell BM, Rabu C, Leznicki P, Young JC, High S (2007) Post-translational integration of tail-anchored proteins is facilitated by defined molecular chaperones. J Cell Sci 120:1743-1751.
    • (2007) J Cell Sci , vol.120 , pp. 1743-1751
    • Abell, B.M.1    Rabu, C.2    Leznicki, P.3    Young, J.C.4    High, S.5
  • 9
    • 46749104133 scopus 로고    scopus 로고
    • Distinct targeting pathways for the membrane insertion of tail-anchored (TA) proteins
    • Favaloro V, Spasic M, Schwappach B, Dobberstein B (2008) Distinct targeting pathways for the membrane insertion of tail-anchored (TA) proteins. J Cell Sci 121:1832-1840.
    • (2008) J Cell Sci , vol.121 , pp. 1832-1840
    • Favaloro, V.1    Spasic, M.2    Schwappach, B.3    Dobberstein, B.4
  • 10
    • 33947218544 scopus 로고    scopus 로고
    • Identification of a targeting factor for posttranslational membrane protein insertion into the ER
    • Stefanovic S, Hegde RS (2007) Identification of a targeting factor for posttranslational membrane protein insertion into the ER. Cell 128:1147-1159.
    • (2007) Cell , vol.128 , pp. 1147-1159
    • Stefanovic, S.1    Hegde, R.S.2
  • 11
    • 0028216609 scopus 로고
    • Targeting of passenger protein domains to multiple intracellular membranes
    • Janiak F, Glover JR, Leber B, Rachubinski RA, Andrews DW (1994) Targeting of passenger protein domains to multiple intracellular membranes. Biochem J 300:191-199.
    • (1994) Biochem J , vol.300 , pp. 191-199
    • Janiak, F.1    Glover, J.R.2    Leber, B.3    Rachubinski, R.A.4    Andrews, D.W.5
  • 12
    • 0030587453 scopus 로고    scopus 로고
    • Isolation of the ATP-binding human homolog of the arsA component of the bacterial arsenite transporter
    • Kurdi-Haidar B, et al. (1996) Isolation of the ATP-binding human homolog of the arsA component of the bacterial arsenite transporter. Genomics 36:486-491.
    • (1996) Genomics , vol.36 , pp. 486-491
    • Kurdi-Haidar, B.1
  • 13
    • 0037412034 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae Arr4p is involved in metal and heat tolerance
    • Shen J, Hsu CM, Kang BK, Rosen BP, Bhattacharjee H (2003) The Saccharomyces cerevisiae Arr4p is involved in metal and heat tolerance. Biometals 16:369-378.
    • (2003) Biometals , vol.16 , pp. 369-378
    • Shen, J.1    Hsu, C.M.2    Kang, B.K.3    Rosen, B.P.4    Bhattacharjee, H.5
  • 14
    • 0345713152 scopus 로고    scopus 로고
    • Disruption of six Saccharomyces cerevisiae novel genes and phenotypic analysis of the deletants
    • Zuniga S, Boskovic J, Jimenez A, Ballesta JP, Remacha M (1999) Disruption of six Saccharomyces cerevisiae novel genes and phenotypic analysis of the deletants. Yeast 15:945-953.
    • (1999) Yeast , vol.15 , pp. 945-953
    • Zuniga, S.1    Boskovic, J.2    Jimenez, A.3    Ballesta, J.P.4    Remacha, M.5
  • 16
    • 49549086224 scopus 로고    scopus 로고
    • The GET complex mediates insertion of tail-anchored proteins into the ER membrane
    • Schuldiner M, et al. (2008) The GET complex mediates insertion of tail-anchored proteins into the ER membrane. Cell 134:634-645.
    • (2008) Cell , vol.134 , pp. 634-645
    • Schuldiner, M.1
  • 17
    • 63449128473 scopus 로고    scopus 로고
    • Comprehensive characterization of genes required for protein folding in the endoplasmic reticulum
    • Jonikas MC, et al. (2009) Comprehensive characterization of genes required for protein folding in the endoplasmic reticulum. Science 323:1693-1697.
    • (2009) Science , vol.323 , pp. 1693-1697
    • Jonikas, M.C.1
  • 18
    • 34250219575 scopus 로고    scopus 로고
    • Membrane protein chaperones: A new twist in the tail?
    • Rabu C, High S (2007) Membrane protein chaperones: A new twist in the tail? Curr Biol 17:R472-R474.
    • (2007) Curr Biol , vol.17
    • Rabu, C.1    High, S.2
  • 19
    • 0036295212 scopus 로고    scopus 로고
    • Classification and evolution of P-loop GTPases and related ATPases
    • Leipe DD, Wolf YI, Koonin EV, Aravind L (2002) Classification and evolution of P-loop GTPases and related ATPases. J Mol Biol 317:41-72.
    • (2002) J Mol Biol , vol.317 , pp. 41-72
    • Leipe, D.D.1    Wolf, Y.I.2    Koonin, E.V.3    Aravind, L.4
  • 20
    • 0034282542 scopus 로고    scopus 로고
    • Structure of the ArsA ATPase: The catalytic subunit of a heavy metal resistance pump
    • Zhou T, Radaev S, Rosen BP, Gatti DL (2000) Structure of the ArsA ATPase: The catalytic subunit of a heavy metal resistance pump. EMBO J 19:4838-4845.
    • (2000) EMBO J , vol.19 , pp. 4838-4845
    • Zhou, T.1    Radaev, S.2    Rosen, B.P.3    Gatti, D.L.4
  • 21
    • 0035839434 scopus 로고    scopus 로고
    • Conformational changes in four regions of the Escherichia coli ArsA ATPase link ATP hydrolysis to ion translocation
    • Zhou T, Radaev S, Rosen BP, Gatti DL (2001) Conformational changes in four regions of the Escherichia coli ArsA ATPase link ATP hydrolysis to ion translocation. J Biol Chem 276:30414-30422.
    • (2001) J Biol Chem , vol.276 , pp. 30414-30422
    • Zhou, T.1    Radaev, S.2    Rosen, B.P.3    Gatti, D.L.4
  • 22
    • 0031017523 scopus 로고    scopus 로고
    • Structure of the conserved GTPase domain of the signal recognition particle
    • Freymann DM, Keenan RJ, Stroud RM, Walter P (1997) Structure of the conserved GTPase domain of the signal recognition particle. Nature 385:361-364.
    • (1997) Nature , vol.385 , pp. 361-364
    • Freymann, D.M.1    Keenan, R.J.2    Stroud, R.M.3    Walter, P.4
  • 23
    • 0031030085 scopus 로고    scopus 로고
    • Crystal structure of the NG domain from the signal-recognition particle receptor FtsY
    • Montoya G, Svensson C, Luirink J, Sinning I (1997) Crystal structure of the NG domain from the signal-recognition particle receptor FtsY. Nature 385:365-368.
    • (1997) Nature , vol.385 , pp. 365-368
    • Montoya, G.1    Svensson, C.2    Luirink, J.3    Sinning, I.4
  • 24
    • 35348904908 scopus 로고    scopus 로고
    • The crystal structure of the third signal-recognition particle GTPase FlhF reveals a homodimer with bound GTP
    • Bange G, Petzold G, Wild K, Parlitz RO, Sinning I (2007) The crystal structure of the third signal-recognition particle GTPase FlhF reveals a homodimer with bound GTP. Proc Natl Acad Sci USA 104:13621-13625.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 13621-13625
    • Bange, G.1    Petzold, G.2    Wild, K.3    Parlitz, R.O.4    Sinning, I.5
  • 25
    • 34547929138 scopus 로고    scopus 로고
    • Conformational changes in the GTPase modules of the signal reception particle and its receptor drive initiation of protein translocation
    • Shan SO, Chandrasekar S, Walter P (2007) Conformational changes in the GTPase modules of the signal reception particle and its receptor drive initiation of protein translocation. J Cell Biol 178:611-620.
    • (2007) J Cell Biol , vol.178 , pp. 611-620
    • Shan, S.O.1    Chandrasekar, S.2    Walter, P.3
  • 26
    • 36048962750 scopus 로고    scopus 로고
    • Protein translocation: Checkpoint role for SRP GTPase activation
    • Bange G, Wild K, Sinning I (2007) Protein translocation: Checkpoint role for SRP GTPase activation. Curr Biol 17:R980-R982.
    • (2007) Curr Biol , vol.17
    • Bange, G.1    Wild, K.2    Sinning, I.3
  • 27
    • 0023740734 scopus 로고
    • Integration of membrane proteins into the endoplasmic reticulum requires GTP
    • Wilson C, Connolly T, Morrison T, Gilmore R (1988) Integration of membrane proteins into the endoplasmic reticulum requires GTP. J Cell Biol 107:69-77.
    • (1988) J Cell Biol , vol.107 , pp. 69-77
    • Wilson, C.1    Connolly, T.2    Morrison, T.3    Gilmore, R.4
  • 28
    • 70349595267 scopus 로고    scopus 로고
    • Protein targeting by the signal recognition particle
    • Grudnik P, Bange G, Sinning I (2009) Protein targeting by the signal recognition particle. Biol Chem 390(8):775-782.
    • (2009) Biol Chem , vol.390 , Issue.8 , pp. 775-782
    • Grudnik, P.1    Bange, G.2    Sinning, I.3
  • 29
    • 70349272618 scopus 로고    scopus 로고
    • The structural basis of tail- anchoredmembraneprotein recognition by Get3
    • doi:10.1038/ nature08319
    • Mateja A, et al. (2009) The structural basis of tail- anchoredmembraneprotein recognition by Get3. Nature, doi:10.1038/ nature08319.
    • (2009) Nature
    • Mateja, A.1
  • 30
    • 70349299919 scopus 로고    scopus 로고
    • Model for eukaryotic tail-anchored protein binding based on the structure of Get3
    • Suloway CJ, Chartron JW, Zaslaver M, Clemons WM, Jr. (2009) Model for eukaryotic tail-anchored protein binding based on the structure of Get3. Proc Natl Acad Sci USA 106:14849-14854.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 14849-14854
    • Suloway, C.J.1    Chartron, J.W.2    Zaslaver, M.3    Clemons Jr., W.M.4
  • 31
    • 0038121525 scopus 로고    scopus 로고
    • Analysis of protein complexes with hydrogen exchange and mass spectrometry
    • Engen JR (2003) Analysis of protein complexes with hydrogen exchange and mass spectrometry. Analyst 128:623-628.
    • (2003) Analyst , vol.128 , pp. 623-628
    • Engen, J.R.1
  • 32
    • 62049084010 scopus 로고    scopus 로고
    • Spatially and kinetically resolved changes in the conformational dynamics of the Hsp90 chaperone machine
    • Graf C, Stankiewicz M, Kramer G, Mayer MP (2009) Spatially and kinetically resolved changes in the conformational dynamics of the Hsp90 chaperone machine. EMBO J 28:602-613.
    • (2009) EMBO J , vol.28 , pp. 602-613
    • Graf, C.1    Stankiewicz, M.2    Kramer, G.3    Mayer, M.P.4
  • 33
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E, Henrick K (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372:774-797.
    • (2007) J Mol Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 34
    • 0026662162 scopus 로고
    • Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii
    • Georgiadis MM, et al. (1992) Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii. Science 257:1653-1659.
    • (1992) Science , vol.257 , pp. 1653-1659
    • Georgiadis, M.M.1
  • 37
    • 33644852489 scopus 로고    scopus 로고
    • The yeast Arr4p ATPase binds the chloride transporter Gef1p when copper is available in the cytosol
    • Metz J, Wachter A, Schmidt B, Bujnicki JM, Schwappach B (2006) The yeast Arr4p ATPase binds the chloride transporter Gef1p when copper is available in the cytosol. J Biol Chem 281:410-417.
    • (2006) J Biol Chem , vol.281 , pp. 410-417
    • Metz, J.1    Wachter, A.2    Schmidt, B.3    Bujnicki, J.M.4    Schwappach, B.5
  • 39
    • 13444281991 scopus 로고    scopus 로고
    • Bacterial chromosome segregation: Structure and DNA binding of the Soj dimer - A conserved biological switch
    • Leonard TA, Butler PJ, Lowe J (2005) Bacterial chromosome segregation: Structure and DNA binding of the Soj dimer - A conserved biological switch. EMBO J 24:270-282.
    • (2005) EMBO J , vol.24 , pp. 270-282
    • Leonard, T.A.1    Butler, P.J.2    Lowe, J.3
  • 40
    • 0035901493 scopus 로고    scopus 로고
    • Structural and functional studies of MinD ATPase: Implications for the molecular recognition of the bacterial cell division apparatus
    • Hayashi I, Oyama T, Morikawa K (2001) Structural and functional studies of MinD ATPase: Implications for the molecular recognition of the bacterial cell division apparatus. EMBO J 20:1819-1828.
    • (2001) EMBO J , vol.20 , pp. 1819-1828
    • Hayashi, I.1    Oyama, T.2    Morikawa, K.3
  • 41
    • 0032510685 scopus 로고    scopus 로고
    • Snapshot of a phosphorylated substrate intermediate by kinetic crystallography
    • Kack H, Gibson KJ, Lindqvist Y, Schneider G (1998) Snapshot of a phosphorylated substrate intermediate by kinetic crystallography. Proc Natl Acad Sci USA 95:5495-5500.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5495-5500
    • Kack, H.1    Gibson, K.J.2    Lindqvist, Y.3    Schneider, G.4
  • 42
    • 0032563163 scopus 로고    scopus 로고
    • Crystal structure of the signal sequence binding subunit of the signal recognition particle
    • Keenan RJ, Freymann DM, Walter P, Stroud RM (1998) Crystal structure of the signal sequence binding subunit of the signal recognition particle. Cell 94:181-191.
    • (1998) Cell , vol.94 , pp. 181-191
    • Keenan, R.J.1    Freymann, D.M.2    Walter, P.3    Stroud, R.M.4
  • 43
    • 0344304454 scopus 로고    scopus 로고
    • Crystal structure of the complete core of archaeal signal recognition particle and implications for interdomain communication
    • Rosendal KR, Wild K, Montoya G, Sinning I (2003) Crystal structure of the complete core of archaeal signal recognition particle and implications for interdomain communication. Proc Natl Acad Sci USA 100:14701-14706.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 14701-14706
    • Rosendal, K.R.1    Wild, K.2    Montoya, G.3    Sinning, I.4
  • 44
    • 0345803934 scopus 로고    scopus 로고
    • Mapping temperature-induced conformational changes in the Escherichia coli heat shock transcription factor sigma 32 by amide hydrogen exchange
    • Rist W, Jorgensen TJ, Roepstorff P, Bukau B, Mayer MP (2003) Mapping temperature-induced conformational changes in the Escherichia coli heat shock transcription factor sigma 32 by amide hydrogen exchange. J Biol Chem 278:51415-51421.
    • (2003) J Biol Chem , vol.278 , pp. 51415-51421
    • Rist, W.1    Jorgensen, T.J.2    Roepstorff, P.3    Bukau, B.4    Mayer, M.P.5
  • 45
    • 33745183353 scopus 로고    scopus 로고
    • Amide hydrogen exchange reveals conformational changes in hsp70 chaperones important for allosteric regulation
    • Rist W, Graf C, Bukau B, Mayer MP (2006) Amide hydrogen exchange reveals conformational changes in hsp70 chaperones important for allosteric regulation. J Biol Chem 281:16493-16501.
    • (2006) J Biol Chem , vol.281 , pp. 16493-16501
    • Rist, W.1    Graf, C.2    Bukau, B.3    Mayer, M.P.4
  • 46
    • 0035969987 scopus 로고    scopus 로고
    • Changes in protein conformational mobility upon activation of extracellular regulated protein kinase-2 as detected by hydrogen exchange
    • Hoofnagle AN, Resing KA, Goldsmith EJ, Ahn NG (2001) Changes in protein conformational mobility upon activation of extracellular regulated protein kinase-2 as detected by hydrogen exchange. Proc Natl Acad Sci USA 98:956-961.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 956-961
    • Hoofnagle, A.N.1    Resing, K.A.2    Goldsmith, E.J.3    Ahn, N.G.4
  • 47
    • 0030046197 scopus 로고    scopus 로고
    • Amide hydrogen exchange determined by mass spectrometry: Application to rabbit muscle aldolase
    • Zhang Z, Post CB, Smith DL (1996) Amide hydrogen exchange determined by mass spectrometry: Application to rabbit muscle aldolase. Biochemistry 35:779-791.
    • (1996) Biochemistry , vol.35 , pp. 779-791
    • Zhang, Z.1    Post, C.B.2    Smith, D.L.3
  • 48
    • 0032575478 scopus 로고    scopus 로고
    • Biochemical characterization of the human arsenite-stimulated ATPase (hASNA-I)
    • Kurdi-Haidar B, Heath D, Aebi S, Howell SB (1998) Biochemical characterization of the human arsenite-stimulated ATPase (hASNA-I). J Biol Chem 273:22173-22176.
    • (1998) J Biol Chem , vol.273 , pp. 22173-22176
    • Kurdi-Haidar, B.1    Heath, D.2    Aebi, S.3    Howell, S.B.4
  • 49
    • 0034598967 scopus 로고    scopus 로고
    • Trimeric ring-like structure of ArsA ATPase
    • Wang HW, et al. (2000) Trimeric ring-like structure of ArsA ATPase. FEBS Lett 469:105-110.
    • (2000) FEBS Lett , vol.469 , pp. 105-110
    • Wang, H.W.1
  • 50
    • 33746537716 scopus 로고    scopus 로고
    • A structural analysis of asymmetry required for catalytic activity of an ABC-ATPase domain dimer
    • Zaitseva J, et al. (2006) A structural analysis of asymmetry required for catalytic activity of an ABC-ATPase domain dimer. EMBO J 25:3432-3443.
    • (2006) EMBO J , vol.25 , pp. 3432-3443
    • Zaitseva, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.