메뉴 건너뛰기




Volumn 31, Issue 15, 2012, Pages 3282-3296

Erratum: BiP-mediated closing of the Sec61 channel limits Ca 2+ leakage from the ER (The EMBO Journal (2012) 31 (3282-3296) DOI: 10.1038/emboj.2012.189);BiP-mediated closing of the Sec61 channel limits Ca 2+ leakage from the ER

Author keywords

BiP; calcium homeostasis; diabetes mutation; endoplasmic reticulum; ER calcium leakage; Sec61 complex gating

Indexed keywords

CALCIUM ION; CALRETICULIN; CHAPERONE; GLUCOSE REGULATED PROTEIN 78; MEMBRANE PROTEIN; PROTEIN SEC61A1; TYROSINE; UNCLASSIFIED DRUG;

EID: 84864877220     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/emboj.2012.243     Document Type: Erratum
Times cited : (132)

References (56)
  • 1
    • 13444271726 scopus 로고    scopus 로고
    • The molecular mechanisms underlying BiP-mediated gating of the Sec61 translocon of the endoplasmic reticulum
    • Alder NN, Shen Y, Brodsky JL, Hendershot LM, Johnson AE (2005) The molecular mechanisms underlying BiP-mediated gating of the Sec61 translocon of the endoplasmic reticulum. J Cell Biol 168: 389-399
    • (2005) J Cell Biol , vol.168 , pp. 389-399
    • Alder, N.N.1    Shen, Y.2    Brodsky, J.L.3    Hendershot, L.M.4    Johnson, A.E.5
  • 2
    • 39549101755 scopus 로고    scopus 로고
    • BiP mutants that are unable to interact with endoplasmic reticulum DnaJ proteins provide insight into interdomain interactions of BiP
    • Awad W, Estrada I, Shen Y, Hendershot LM (2008) BiP mutants that are unable to interact with endoplasmic reticulum DnaJ proteins provide insight into interdomain interactions of BiP. Proc Natl Acad Sci USA 105: 1164-1169
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 1164-1169
    • Awad, W.1    Estrada, I.2    Shen, Y.3    Hendershot, L.M.4
  • 4
    • 0036877142 scopus 로고    scopus 로고
    • The endoplasmic reticulum: A multifunctional signalling organelle
    • Berridge MJ (2002) The endoplasmic reticulum: a multifunctional signalling organelle. Cell Calcium 32: 235-249
    • (2002) Cell Calcium , vol.32 , pp. 235-249
    • Berridge, M.J.1
  • 5
    • 0016753216 scopus 로고
    • Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma
    • Blobel G, Dobberstein B (1975) Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma. J Cell Biol 67: 835-851
    • (1975) J Cell Biol , vol.67 , pp. 835-851
    • Blobel, G.1    Dobberstein, B.2
  • 6
    • 0036878788 scopus 로고    scopus 로고
    • Calcium leak from intracellular stores-The enigma of calcium signalling
    • Camello C, Lomax R, Petersen OH (2002) Calcium leak from intracellular stores-the enigma of calcium signalling. Cell Calcium 32: 355-361
    • (2002) Cell Calcium , vol.32 , pp. 355-361
    • Camello, C.1    Lomax, R.2    Petersen, O.H.3
  • 7
    • 0027985063 scopus 로고
    • Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore
    • Crowley KS, Liao S, Worrell VE, Reinhart GD, Johnson AE (1994) Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore. Cell 78: 461-471
    • (1994) Cell , vol.78 , pp. 461-471
    • Crowley, K.S.1    Liao, S.2    Worrell, V.E.3    Reinhart, G.D.4    Johnson, A.E.5
  • 9
    • 0033521072 scopus 로고    scopus 로고
    • Setting the standards: Quality control in the secretory pathway
    • Ellgaard L, Molinari M, Helenius A (1999) Setting the standards: quality control in the secretory pathway. Science 286: 1882-1888
    • (1999) Science , vol.286 , pp. 1882-1888
    • Ellgaard, L.1    Molinari, M.2    Helenius, A.3
  • 12
    • 33845656359 scopus 로고    scopus 로고
    • Passive calcium leak via translocon is a first step for iPLA2-pathway regulated store operated channels activation
    • Flourakis M, Van Coppenolle F, Lehen'kyi V, Beck B, Skryma R (2006) Passive calcium leak via translocon is a first step for iPLA2-pathway regulated store operated channels activation. FASEB J 20: 1215-1217
    • (2006) FASEB J , vol.20 , pp. 1215-1217
    • Flourakis, M.1    Van Coppenolle, F.2    Lehen'Kyi, V.3    Beck, B.4    Skryma, R.5
  • 13
    • 0028149893 scopus 로고
    • Common and divergent peptide binding specificities of hsp70 moecular chaperones
    • Fourie AM, Sambrook JF, Gething M-JH (1994) Common and divergent peptide binding specificities of hsp70 moecular chaperones. J Biol Chem 269: 30470-30478
    • (1994) J Biol Chem , vol.269 , pp. 30470-30478
    • Fourie, A.M.1    Sambrook, J.F.2    Gething, M.-J.H.3
  • 14
    • 34248573016 scopus 로고    scopus 로고
    • Both translocon and a cation channel are involved in the passive Ca2 + leak from the endoplasmic reticulum: A mechanistic study on rat liver microsomes
    • Giunti R, Gamberucci A, Fulceri R, Banhegyi G (2007) Both translocon and a cation channel are involved in the passive Ca2 + leak from the endoplasmic reticulum: a mechanistic study on rat liver microsomes. Arch Biochem Biophys 462: 115-121
    • (2007) Arch Biochem Biophys , vol.462 , pp. 115-121
    • Giunti, R.1    Gamberucci, A.2    Fulceri, R.3    Banhegyi, G.4
  • 15
    • 0027424601 scopus 로고
    • Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane
    • Görlich D, Rapoport TA (1993) Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane. Cell 75: 615-630
    • (1993) Cell , vol.75 , pp. 615-630
    • Görlich, D.1    Rapoport, T.A.2
  • 16
    • 0021895138 scopus 로고
    • A new generation of Ca2 + indicators with greatly improved fluorescence properties
    • Grynkiewicz G, Poeni M, Tsien RY (1985) A new generation of Ca2 + indicators with greatly improved fluorescence properties. J Biol Chem 260: 3440-3450
    • (1985) J Biol Chem , vol.260 , pp. 3440-3450
    • Grynkiewicz, G.1    Poeni, M.2    Tsien, R.Y.3
  • 17
    • 34848895197 scopus 로고    scopus 로고
    • Structural determinants of lateral gate opening in the protein translocon
    • Gumbart J, Schulten K (2007) Structural determinants of lateral gate opening in the protein translocon. Biochemistry 46: 11147-11157
    • (2007) Biochemistry , vol.46 , pp. 11147-11157
    • Gumbart, J.1    Schulten, K.2
  • 18
  • 19
    • 0037148535 scopus 로고    scopus 로고
    • A new role for BiP: Closing the aqueous translocon pore during protein integration into the ER membrane
    • Haigh NG, Johnson AE (2002) A new role for BiP: closing the aqueous translocon pore during protein integration into the ER membrane. J Cell Biol 156: 261-270
    • (2002) J Cell Biol , vol.156 , pp. 261-270
    • Haigh, N.G.1    Johnson, A.E.2
  • 20
    • 0030611388 scopus 로고    scopus 로고
    • The aqueous pore through the translocon has a diameter of 40-60 A during cotranslational protein translocation at the ER membrane
    • Hamman BD, Chen JC, Johnson AE (1997) The aqueous pore through the translocon has a diameter of 40-60 A during cotranslational protein translocation at the ER membrane. Cell 89: 535-544
    • (1997) Cell , vol.89 , pp. 535-544
    • Hamman, B.D.1    Chen, J.C.2    Johnson, A.E.3
  • 21
    • 0032549767 scopus 로고    scopus 로고
    • BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation
    • Hamman BD, Hendershot LM, Johnson AE (1998) BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation. Cell 92: 747-758
    • (1998) Cell , vol.92 , pp. 747-758
    • Hamman, B.D.1    Hendershot, L.M.2    Johnson, A.E.3
  • 22
    • 79960829351 scopus 로고    scopus 로고
    • Calmodulin regulation of the calcium-leak channel Sec61 is unique to vertebrates
    • Harsman A, Kopp A, Wagner R, Zimmermann R, Jung M (2011) Calmodulin regulation of the calcium-leak channel Sec61 is unique to vertebrates. Channels 5: 293-298
    • (2011) Channels , vol.5 , pp. 293-298
    • Harsman, A.1    Kopp, A.2    Wagner, R.3    Zimmermann, R.4    Jung, M.5
  • 23
    • 0027958547 scopus 로고
    • Evolutionary conservation of components of the protein translocation complex
    • Hartmann E, Sommer T, Prehn S, Gorlich D, Jentsch S, Rapoport TA (1994) Evolutionary conservation of components of the protein translocation complex. Nature 367: 654-657
    • (1994) Nature , vol.367 , pp. 654-657
    • Hartmann, E.1    Sommer, T.2    Prehn, S.3    Gorlich, D.4    Jentsch, S.5    Rapoport, T.A.6
  • 24
    • 0026659680 scopus 로고
    • The endoplasmic reticulum as a protein-folding compartment
    • Helenius A, Marquardt T, Braakman I (1992) The endoplasmic reticulum as a protein-folding compartment. Trends Cell Biol 2: 227-231
    • (1992) Trends Cell Biol , vol.2 , pp. 227-231
    • Helenius, A.1    Marquardt, T.2    Braakman, I.3
  • 25
    • 34250721648 scopus 로고    scopus 로고
    • Peptide arrays on cellulose support: SPOT synthesis a time and cost efficient method for synthesis of large numbers of peptides in a parallel and addressable fashion
    • Hilpert K, Winkler DF, Hancock RE (2007) Peptide arrays on cellulose support: SPOT synthesis, a time and cost efficient method for synthesis of large numbers of peptides in a parallel and addressable fashion. Nat Protoc 2: 1333-1349
    • (2007) Nat Protoc , vol.2 , pp. 1333-1349
    • Hilpert, K.1    Winkler, D.F.2    Hancock, R.E.3
  • 27
    • 0036481454 scopus 로고    scopus 로고
    • Cotranslational partitioning of nascent prion protein into multiple populations at the translocation channel
    • Kim SJ, Mitra D, Salerno JR, Hegde RS (2002) Cotranslational partitioning of nascent prion protein into multiple populations at the translocation channel. Dev Cell 2: 207-217
    • (2002) Dev Cell , vol.2 , pp. 207-217
    • Kim, S.J.1    Mitra, D.2    Salerno, J.R.3    Hegde, R.S.4
  • 28
    • 0025740247 scopus 로고
    • A microsomal protein is involved in ATP-dependent transport of presecretory proteins into mammalian microsomes
    • Klappa P, Mayinger P, Pipkorn R, Zimmermann M, Zimmermann R (1991) A microsomal protein is involved in ATP-dependent transport of presecretory proteins into mammalian microsomes. EMBO J 10: 2795-2803
    • (1991) EMBO J , vol.10 , pp. 2795-2803
    • Klappa, P.1    Mayinger, P.2    Pipkorn, R.3    Zimmermann, M.4    Zimmermann, R.5
  • 31
    • 80355132752 scopus 로고    scopus 로고
    • Live cell calcium imaging combined with siRNA mediated gene silencing identifies Ca2 + leak channels in the ER membrane and their regulatory mechanisms
    • Lang S, Schäuble N, Cavalié A, Zimmermann R (2011b) Live cell calcium imaging combined with siRNA mediated gene silencing identifies Ca2 + leak channels in the ER membrane and their regulatory mechanisms. JoVE 53: e2730
    • (2011) JoVE , vol.53
    • Lang, S.1    Schäuble, N.2    Cavalié, A.3    Zimmermann, R.4
  • 32
    • 77449130121 scopus 로고    scopus 로고
    • A point mutation in Sec61a1 leads to diabetes and hepatosteatosis in mice
    • Lloyd DJ, Wheeler MC, Gekakis N (2010) A point mutation in Sec61a1 leads to diabetes and hepatosteatosis in mice. Diabetes 59: 460-470
    • (2010) Diabetes , vol.59 , pp. 460-470
    • Lloyd, D.J.1    Wheeler, M.C.2    Gekakis, N.3
  • 33
    • 0037135534 scopus 로고    scopus 로고
    • Basal and physiological Ca2 + leak from the endoplasmic reticulum of pancreatic acinar cells. Second messenger-activated channels and translocons
    • Lomax RB, Camello C, Van Coppenolle F, Petersen OH (2002) Basal and physiological Ca2 + leak from the endoplasmic reticulum of pancreatic acinar cells. Second messenger-activated channels and translocons. J Biol Chem 277: 26479-26485
    • (2002) J Biol Chem , vol.277 , pp. 26479-26485
    • Lomax, R.B.1    Camello, C.2    Van Coppenolle, F.3    Petersen, O.H.4
  • 36
    • 0027238583 scopus 로고
    • Lumenal proteins of the mammalien endoplasmic reticulum are required to complete protein translocation
    • Nicchitta CV, Blobel G (1993) Lumenal proteins of the mammalien endoplasmic reticulum are required to complete protein translocation. Cell 73: 989-998
    • (1993) Cell , vol.73 , pp. 989-998
    • Nicchitta, C.V.1    Blobel, G.2
  • 37
    • 33847136350 scopus 로고    scopus 로고
    • Intracellular Ca2 + release via the ER translocon activates store-operated calcium entry
    • Ong HL, Liu X, Sharma A, Hegde RS, Ambudkar IS (2007) Intracellular Ca2 + release via the ER translocon activates store-operated calcium entry. Pflugers Arch 453: 797-808
    • (2007) Pflugers Arch , vol.453 , pp. 797-808
    • Ong, H.L.1    Liu, X.2    Sharma, A.3    Hegde, R.S.4    Ambudkar, I.S.5
  • 38
    • 79955901001 scopus 로고    scopus 로고
    • Preserving the membrane barrier for small molecules during bacterial protein translocation
    • Park E, Rapoport TA (2011) Preserving the membrane barrier for small molecules during bacterial protein translocation. Nature 473: 239-242
    • (2011) Nature , vol.473 , pp. 239-242
    • Park, E.1    Rapoport, T.A.2
  • 40
    • 49749136198 scopus 로고    scopus 로고
    • A non-disruptive strategy to target calcium indicator dyes to the endoplasmic reticulum
    • Rehberg M, Lepier A, Solchenberger B, Osten P, Blum R (2008) A non-disruptive strategy to target calcium indicator dyes to the endoplasmic reticulum. Cell Calcium 44: 386-399
    • (2008) Cell Calcium , vol.44 , pp. 386-399
    • Rehberg, M.1    Lepier, A.2    Solchenberger, B.3    Osten, P.4    Blum, R.5
  • 41
    • 33644847375 scopus 로고    scopus 로고
    • Microdomains of intracellular Ca2 +: Molecular determinants and functional consequences
    • Rizzuto R, Pozzan T (2006) Microdomains of intracellular Ca2 +: molecular determinants and functional consequences. Physiol Rev 86: 369-408
    • (2006) Physiol Rev , vol.86 , pp. 369-408
    • Rizzuto, R.1    Pozzan, T.2
  • 42
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • Schröder M, Kaufman RJ (2005) The mammalian unfolded protein response. Ann Rev Biochem 74: 739-789
    • (2005) Ann Rev Biochem , vol.74 , pp. 739-789
    • Schröder, M.1    Kaufman, R.J.2
  • 43
    • 26444571807 scopus 로고    scopus 로고
    • Regulation of protein compartmentalization expands the diversity of protein function
    • Shaffer KL, Sharma A, Snapp EL, Hegde RS (2005) Regulation of protein compartmentalization expands the diversity of protein function. Dev Cell 9: 545-554
    • (2005) Dev Cell , vol.9 , pp. 545-554
    • Shaffer, K.L.1    Sharma, A.2    Snapp, E.L.3    Hegde, R.S.4
  • 44
    • 79954426157 scopus 로고    scopus 로고
    • Signaling cell death from the endoplasmic reticulum stress response
    • Shore GC, Papa FR, Oakes SA (2011) Signaling cell death from the endoplasmic reticulum stress response. Curr Opin Cell Biol 23: 143-149
    • (2011) Curr Opin Cell Biol , vol.23 , pp. 143-149
    • Shore, G.C.1    Papa, F.R.2    Oakes, S.A.3
  • 45
    • 80052237952 scopus 로고    scopus 로고
    • Translocation channel gating kinetics balances protein translocation efficiency with signal sequence recognition fidelity
    • Trueman SF, Mandon EC, Gilmore R (2011) Translocation channel gating kinetics balances protein translocation efficiency with signal sequence recognition fidelity. Mol Biol Cell 22: 2983-2993
    • (2011) Mol Biol Cell , vol.22 , pp. 2983-2993
    • Trueman, S.F.1    Mandon, E.C.2    Gilmore, R.3
  • 46
    • 0038786906 scopus 로고    scopus 로고
    • Polypeptide-binding proteins mediate completion of cotranslational protein translocation into the mammalian endoplasmic reticulum
    • Tyedmers J, Lerner M, Wiedmann M, Volkmer J, Zimmermann R (2003) Polypeptide-binding proteins mediate completion of cotranslational protein translocation into the mammalian endoplasmic reticulum. EMBO Rep 4: 505-510
    • (2003) EMBO Rep , vol.4 , pp. 505-510
    • Tyedmers, J.1    Lerner, M.2    Wiedmann, M.3    Volkmer, J.4    Zimmermann, R.5
  • 49
    • 34748918368 scopus 로고    scopus 로고
    • The Hsp70-molecular chaperone network in the pancreatic endoplasmic reticulum: A quantitative approach
    • Weitzmann A, Baldes C, Dudek J, Zimmermann R (2007) The Hsp70-molecular chaperone network in the pancreatic endoplasmic reticulum: a quantitative approach. FEBS J 274: 5175-5187
    • (2007) FEBS J , vol.274 , pp. 5175-5187
    • Weitzmann, A.1    Baldes, C.2    Dudek, J.3    Zimmermann, R.4
  • 50
    • 0030812436 scopus 로고    scopus 로고
    • Molecular architecture of the ER translocase probed by chemical crosslinking of Sss1p to complementary fragments of Sec61p
    • Wilkinson BM, Esnault Y, Craven RA, Skiba F, Fieschi J, Kepès F, Sirling CJ (1997) Molecular architecture of the ER translocase probed by chemical crosslinking of Sss1p to complementary fragments of Sec61p. EMBO J 16: 4549-4559
    • (1997) EMBO J , vol.16 , pp. 4549-4559
    • Wilkinson, B.M.1    Esnault, Y.2    Craven, R.A.3    Skiba, F.4    Fieschi, J.5    Kepès, F.6    Sirling, C.J.7
  • 51
    • 0029024163 scopus 로고
    • The translocation, folding, assembly, and redoxdependent degradation of secretory an membrane proteins in semi-permeabilized mammalian cells
    • Wilson R, Allen AJ, Oliver J, Brookman JL, High S, Bulleid NJ (1995) The translocation, folding, assembly, and redoxdependent degradation of secretory an membrane proteins in semi-permeabilized mammalian cells. Biochem J 387: 679-687
    • (1995) Biochem J , vol.387 , pp. 679-687
    • Wilson, R.1    Allen, A.J.2    Oliver, J.3    Brookman, J.L.4    High, S.5    Bulleid, N.J.6
  • 52
    • 0037665405 scopus 로고    scopus 로고
    • Determinants of the in vivo folding of the prion protein. A bipartite function of helix i in folding and aggregation
    • Winklhofer KF, Heske J, Heller U, Reintjes A, Muranyi W, Moarefi I, Tatzelt J (2003) Determinants of the in vivo folding of the prion protein. A bipartite function of helix I in folding and aggregation. J Biol Chem 278: 14961-14970
    • (2003) J Biol Chem , vol.278 , pp. 14961-14970
    • Winklhofer, K.F.1    Heske, J.2    Heller, U.3    Reintjes, A.4    Muranyi, W.5    Moarefi, I.6    Tatzelt, J.7
  • 54
    • 0036877135 scopus 로고    scopus 로고
    • Molecular physiology of the SERCA and SPCA pumps
    • Wuytack F, Raeymaekers L, Missiaen L (2002) Molecular physiology of the SERCA and SPCA pumps. Cell Calcium 32: 279-305
    • (2002) Cell Calcium , vol.32 , pp. 279-305
    • Wuytack, F.1    Raeymaekers, L.2    Missiaen, L.3
  • 55
    • 0034604674 scopus 로고    scopus 로고
    • Rapid turnover of calcium in the endoplasmic reticulum during signalling. Studies with cameleon calcium indicators
    • Yu R, Hinkle PM (2000) Rapid turnover of calcium in the endoplasmic reticulum during signalling. Studies with cameleon calcium indicators. J Biol Chem 275: 23648-23653
    • (2000) J Biol Chem , vol.275 , pp. 23648-23653
    • Yu, R.1    Hinkle, P.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.