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Volumn 147, Issue 7, 2011, Pages 1576-1588

A calmodulin-dependent translocation pathway for small secretory proteins

Author keywords

[No Author keywords available]

Indexed keywords

CALMODULIN; CHAPERONIN; SECRETORY PROTEIN; SIGNAL PEPTIDE;

EID: 84455178968     PISSN: 00928674     EISSN: 10974172     Source Type: Journal    
DOI: 10.1016/j.cell.2011.11.048     Document Type: Article
Times cited : (104)

References (51)
  • 1
    • 0027759380 scopus 로고
    • A Sec63-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposome
    • J.L. Brodsky, and R. Schekman A Sec63-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposome J. Cell Biol. 123 1993 1355 1363
    • (1993) J. Cell Biol. , vol.123 , pp. 1355-1363
    • Brodsky, J.L.1    Schekman, R.2
  • 2
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    • K.A. Brogden Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat. Rev. Microbiol. 3 2005 238 250
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 3
    • 0023069451 scopus 로고
    • Intracellular Calcium Homeostasis
    • E. Carafoli Intracellular Calcium Homeostasis Annu. Rev. Biochem. 56 1987 395 433
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 395-433
    • Carafoli, E.1
  • 4
    • 0024298706 scopus 로고
    • 70K heat shock related proteins stimulate protein translocation into microsomes
    • W.J. Chirico, M.G. Waters, and G. Blobel 70K heat shock related proteins stimulate protein translocation into microsomes Nature 332 1988 805 810
    • (1988) Nature , vol.332 , pp. 805-810
    • Chirico, W.J.1    Waters, M.G.2    Blobel, G.3
  • 5
    • 0024298711 scopus 로고
    • A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides
    • R.J. Deshaies, B.D. Koch, M. Werner-Washburne, E.A. Craig, and R. Schekman A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides Nature 332 1988 800 805
    • (1988) Nature , vol.332 , pp. 800-805
    • Deshaies, R.J.1    Koch, B.D.2    Werner-Washburne, M.3    Craig, E.A.4    Schekman, R.5
  • 6
    • 0025970051 scopus 로고
    • Assembly of yeast Sec protein involved in translocation into the endoplasmic reticulum into a membrane-bound multisubunit complex
    • R.J. Deshaies, S.L. Sanders, D.A. Feldhelm, and R. Schekman Assembly of yeast Sec protein involved in translocation into the endoplasmic reticulum into a membrane-bound multisubunit complex Nature 349 1991 806 808
    • (1991) Nature , vol.349 , pp. 806-808
    • Deshaies, R.J.1    Sanders, S.L.2    Feldhelm, D.A.3    Schekman, R.4
  • 7
    • 0342995731 scopus 로고    scopus 로고
    • The cotranslational integration of membrane proteins into the phospholipid bilayer is a multistep process
    • H. Do, D. Falcone, J. Lin, D.W. Andrews, and A.E. Johnson The cotranslational integration of membrane proteins into the phospholipid bilayer is a multistep process Cell 85 1996 369 378
    • (1996) Cell , vol.85 , pp. 369-378
    • Do, H.1    Falcone, D.2    Lin, J.3    Andrews, D.W.4    Johnson, A.E.5
  • 8
    • 58149181486 scopus 로고    scopus 로고
    • Hsp104 and ClpB: Protein disaggregating machines
    • S.M. Doyle, and S. Wickner Hsp104 and ClpB: protein disaggregating machines Trends Biochem. Sci. 34 2009 40 48
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 40-48
    • Doyle, S.M.1    Wickner, S.2
  • 9
    • 78650434660 scopus 로고    scopus 로고
    • Compartment-restricted biotinylation reveals novel features of prion protein metabolism in vivo
    • A.B. Emerman, Z.-R. Zhang, O. Chakrabarti, and R.S. Hegde Compartment-restricted biotinylation reveals novel features of prion protein metabolism in vivo Mol. Biol. Cell 21 2010 4325 4337
    • (2010) Mol. Biol. Cell , vol.21 , pp. 4325-4337
    • Emerman, A.B.1    Zhang, Z.-R.2    Chakrabarti, O.3    Hegde, R.S.4
  • 12
    • 0037450802 scopus 로고    scopus 로고
    • Substrate-specific function of the translocon-associated protein complex during translocation across the ER membrane
    • R.D. Fons, B.A. Bogert, and R.S. Hegde Substrate-specific function of the translocon-associated protein complex during translocation across the ER membrane J. Cell Biol. 160 2003 529 539
    • (2003) J. Cell Biol. , vol.160 , pp. 529-539
    • Fons, R.D.1    Bogert, B.A.2    Hegde, R.S.3
  • 13
    • 0023917883 scopus 로고
    • Full-length prepro-α-factor can be translocated across the mammalian microsomal membrane only if translation has not terminated
    • P.D. Garcia, and P. Walter Full-length prepro-α-factor can be translocated across the mammalian microsomal membrane only if translation has not terminated J. Cell Biol. 106 1988 1043 1048
    • (1988) J. Cell Biol. , vol.106 , pp. 1043-1048
    • Garcia, P.D.1    Walter, P.2
  • 14
    • 0025605443 scopus 로고
    • Regulation of insulin gene expression by glucose and calcium in transfected primary islet cultures
    • M.S. German, L.G. Moss, and W.J. Rutter Regulation of insulin gene expression by glucose and calcium in transfected primary islet cultures J. Biol. Chem. 265 1990 22063 22066
    • (1990) J. Biol. Chem. , vol.265 , pp. 22063-22066
    • German, M.S.1    Moss, L.G.2    Rutter, W.J.3
  • 15
    • 0034672006 scopus 로고    scopus 로고
    • In vivo kinetics of protein targeting to the endoplasmic reticulum determined by site-specific phosphorylation
    • V. Goder, P. Crottet, and M. Spiess In vivo kinetics of protein targeting to the endoplasmic reticulum determined by site-specific phosphorylation EMBO J. 19 2000 6704 6712
    • (2000) EMBO J. , vol.19 , pp. 6704-6712
    • Goder, V.1    Crottet, P.2    Spiess, M.3
  • 16
    • 79960637590 scopus 로고    scopus 로고
    • Protein targeting and degradation pathways are coupled for elimination of mislocalized proteins
    • 10.1038/nature10181 in press
    • T. Hessa, A. Sharma, M. Mariappan, H.D. Eshleman, E. Gutierrez, and R.S. Hegde Protein targeting and degradation pathways are coupled for elimination of mislocalized proteins Nature 2011 10.1038/nature10181 in press
    • (2011) Nature
    • Hessa, T.1    Sharma, A.2    Mariappan, M.3    Eshleman, H.D.4    Gutierrez, E.5    Hegde, R.S.6
  • 17
    • 62549134121 scopus 로고    scopus 로고
    • Genome-wide analysis in vivo of translation with nucleotide resolution using ribosome profiling
    • N.T. Ingolia, S. Ghaemmaghami, J.R.S. Newman, and J.S. Weissman Genome-wide analysis in vivo of translation with nucleotide resolution using ribosome profiling Science 324 2009 218 223
    • (2009) Science , vol.324 , pp. 218-223
    • Ingolia, N.T.1    Ghaemmaghami, S.2    Newman, J.R.S.3    Weissman, J.S.4
  • 18
    • 0032563163 scopus 로고    scopus 로고
    • Crystal structure of the signal sequence binding subunit of the signal recognition particle
    • R.J. Keenan, D.M. Freymann, P. Walter, and R.M. Stroud Crystal structure of the signal sequence binding subunit of the signal recognition particle Cell 94 1998 181 191
    • (1998) Cell , vol.94 , pp. 181-191
    • Keenan, R.J.1    Freymann, D.M.2    Walter, P.3    Stroud, R.M.4
  • 19
    • 0005614190 scopus 로고
    • Photocrosslinking of the signal sequence of nascent preprolactin to the 54-kilodalton polypeptide of the signal recognition particle
    • U.C. Krieg, P. Walter, and A.E. Johnson Photocrosslinking of the signal sequence of nascent preprolactin to the 54-kilodalton polypeptide of the signal recognition particle Proc. Natl. Acad. Sci. USA 83 1986 8604 8608
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8604-8608
    • Krieg, U.C.1    Walter, P.2    Johnson, A.E.3
  • 20
    • 0642282263 scopus 로고    scopus 로고
    • Intracellular calcium in signaling human β-defensin-2 expression in oral epithelial cells
    • S. Krisanaprakornkit, D. Jotikasthira, and B.A. Dale Intracellular calcium in signaling human β-defensin-2 expression in oral epithelial cells J. Dent. Res. 82 2003 877 882
    • (2003) J. Dent. Res. , vol.82 , pp. 877-882
    • Krisanaprakornkit, S.1    Jotikasthira, D.2    Dale, B.A.3
  • 21
    • 0030732847 scopus 로고    scopus 로고
    • Signal peptide fragments of preprolactin and HIV-1 p-gp160 interact with calmodulin
    • B. Martoglio, R. Graf, and B. Dobberstein Signal peptide fragments of preprolactin and HIV-1 p-gp160 interact with calmodulin EMBO J. 16 1997 6636 6645
    • (1997) EMBO J. , vol.16 , pp. 6636-6645
    • Martoglio, B.1    Graf, R.2    Dobberstein, B.3
  • 23
    • 0033612302 scopus 로고    scopus 로고
    • BiP acts as a molecular ratchet during posttranslational transport of prepro-α-factor across the ER membrane
    • K.E.S. Matlack, B. Misselwitz, K. Plath, and T.A. Rapoport BiP acts as a molecular ratchet during posttranslational transport of prepro-α-factor across the ER membrane Cell 97 1999 553 564
    • (1999) Cell , vol.97 , pp. 553-564
    • Matlack, K.E.S.1    Misselwitz, B.2    Plath, K.3    Rapoport, T.A.4
  • 24
    • 1242291789 scopus 로고    scopus 로고
    • CHIP: A link between the chaperone and proteasome systems
    • H. McConough, and C. Patterson CHIP: a link between the chaperone and proteasome systems Cell Stress Chap. 8 2003 303 308
    • (2003) Cell Stress Chap. , vol.8 , pp. 303-308
    • McConough, H.1    Patterson, C.2
  • 26
    • 0029952547 scopus 로고    scopus 로고
    • Signal sequences specify the targeting route to the endoplasmic reticulum
    • D.T.W. Ng, J.D. Brown, and P. Walter Signal sequences specify the targeting route to the endoplasmic reticulum J. Cell Biol. 134 1996 269 278
    • (1996) J. Cell Biol. , vol.134 , pp. 269-278
    • Ng, D.T.W.1    Brown, J.D.2    Walter, P.3
  • 27
    • 0027238583 scopus 로고
    • Lumenal proteins of the mammalian endoplasmic reticulum are required to complete protein translocation
    • C.V. Nicchitta, and G. Blobel Lumenal proteins of the mammalian endoplasmic reticulum are required to complete protein translocation Cell 73 1993 989 998
    • (1993) Cell , vol.73 , pp. 989-998
    • Nicchitta, C.V.1    Blobel, G.2
  • 28
    • 0025159272 scopus 로고
    • How calmodulin binds its targets: Sequence independent recognition of amphiphilic α-helices
    • K.T. O'Neil, and W.F. DeGrado How calmodulin binds its targets: sequence independent recognition of amphiphilic α-helices Trends Biochem. Sci. 15 1990 59 64
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 59-64
    • O'Neil, K.T.1    Degrado, W.F.2
  • 30
    • 0028997459 scopus 로고
    • Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2
    • S. Panzner, L. Dreier, E. Hartmann, S. Kostka, and T.A. Rapoport Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2 Cell 81 1995 561 570
    • (1995) Cell , vol.81 , pp. 561-570
    • Panzner, S.1    Dreier, L.2    Hartmann, E.3    Kostka, S.4    Rapoport, T.A.5
  • 32
    • 0017191401 scopus 로고
    • An efficient mRNA-dependent translation system from reticulocyte lysates
    • H.R.B. Pelham, and R.J. Jackson An efficient mRNA-dependent translation system from reticulocyte lysates Eur. J. Biochem. 67 1976 247 256
    • (1976) Eur. J. Biochem. , vol.67 , pp. 247-256
    • Pelham, H.R.B.1    Jackson, R.J.2
  • 33
    • 0346339886 scopus 로고    scopus 로고
    • Calcium triggers β-defensin (hBD-2 and hBD-3) and chemokine macrophage inflammatory protein-3α (MIP-3α/CCL20) expression in monolayers of activated human keratinocytes
    • I. Pernet, C. Reymermier, A. Guezennec, J.E. Branka, J. Guesnet, E. Perrier, C. Dezutter-Dambuyant, D. Schmitt, and J. Viac Calcium triggers β-defensin (hBD-2 and hBD-3) and chemokine macrophage inflammatory protein-3α (MIP-3α/CCL20) expression in monolayers of activated human keratinocytes Exp. Dermatol. 12 2003 755 760
    • (2003) Exp. Dermatol. , vol.12 , pp. 755-760
    • Pernet, I.1    Reymermier, C.2    Guezennec, A.3    Branka, J.E.4    Guesnet, J.5    Perrier, E.6    Dezutter-Dambuyant, C.7    Schmitt, D.8    Viac, J.9
  • 34
    • 0034597099 scopus 로고    scopus 로고
    • Spontaneous release of cytosolic proteins from posttranslational substrates before their transport into the endoplasmic reticulum
    • K. Plath, and T.A. Rapoport Spontaneous release of cytosolic proteins from posttranslational substrates before their transport into the endoplasmic reticulum J. Cell Biol. 151 2000 167 178
    • (2000) J. Cell Biol. , vol.151 , pp. 167-178
    • Plath, K.1    Rapoport, T.A.2
  • 35
    • 0346099350 scopus 로고    scopus 로고
    • Interactions between Sec complex and prepro-α-factor during posttranslational protein transport into the endoplasmic reticulum
    • K. Plath, B.M. Wilkinson, C.J. Stirling, and T.A. Rapoport Interactions between Sec complex and prepro-α-factor during posttranslational protein transport into the endoplasmic reticulum Mol. Biol. Cell 15 2004 1 10
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1-10
    • Plath, K.1    Wilkinson, B.M.2    Stirling, C.J.3    Rapoport, T.A.4
  • 36
    • 36749001066 scopus 로고    scopus 로고
    • Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes
    • T.A. Rapoport Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes Nature 450 2007 663 669
    • (2007) Nature , vol.450 , pp. 663-669
    • Rapoport, T.A.1
  • 37
    • 0023445591 scopus 로고
    • Secretion in yeast: Structural features influencing the post-translational translocation of prepro-α-factor in vitro
    • J.A. Rothblatt, J.R. Webb, G. Ammerer, and D.I. Meyer Secretion in yeast: structural features influencing the post-translational translocation of prepro-α-factor in vitro EMBO J. 6 1987 3455 3463
    • (1987) EMBO J. , vol.6 , pp. 3455-3463
    • Rothblatt, J.A.1    Webb, J.R.2    Ammerer, G.3    Meyer, D.I.4
  • 38
    • 0023305012 scopus 로고
    • Import of frog prepropeptide GLa into microsomes requires ATP but does not involve docking protein or ribosomes
    • G. Schlenstedt, and R. Zimmermann Import of frog prepropeptide GLa into microsomes requires ATP but does not involve docking protein or ribosomes EMBO J. 6 1987 699 703
    • (1987) EMBO J. , vol.6 , pp. 699-703
    • Schlenstedt, G.1    Zimmermann, R.2
  • 39
    • 0025006519 scopus 로고
    • A large presecretory protein translocates both cotranslationally, using signal recognition particle and ribosome, and post-translationally, without these ribonucleoparticles, when synthesized in the presence of mammalian microsomes
    • G. Schlenstedt, G.H. Gudmundsson, H.G. Boman, and R. Zimmermann A large presecretory protein translocates both cotranslationally, using signal recognition particle and ribosome, and post-translationally, without these ribonucleoparticles, when synthesized in the presence of mammalian microsomes J. Biol. Chem. 265 1990 13960 13968
    • (1990) J. Biol. Chem. , vol.265 , pp. 13960-13968
    • Schlenstedt, G.1    Gudmundsson, G.H.2    Boman, H.G.3    Zimmermann, R.4
  • 40
    • 0026472576 scopus 로고
    • Structural requirements for transport of preprocecropinA and related presecretory proteins into mammalian microsomes
    • G. Schlenstedt, G.H. Gudmundsson, H.G. Boman, and R. Zimmermann Structural requirements for transport of preprocecropinA and related presecretory proteins into mammalian microsomes J. Biol. Chem. 267 1992 24328 24332
    • (1992) J. Biol. Chem. , vol.267 , pp. 24328-24332
    • Schlenstedt, G.1    Gudmundsson, G.H.2    Boman, H.G.3    Zimmermann, R.4
  • 41
    • 0030846070 scopus 로고    scopus 로고
    • Early responses to infection: Chemokines as mediators of inflammation
    • N.W. Schluger, and W.N. Rom Early responses to infection: chemokines as mediators of inflammation Curr. Opin. Immunol. 9 1997 504 508
    • (1997) Curr. Opin. Immunol. , vol.9 , pp. 504-508
    • Schluger, N.W.1    Rom, W.N.2
  • 42
    • 14544302354 scopus 로고    scopus 로고
    • Co-translational protein targeting by the signal recognition particle
    • S.-O. Shan, and P. Walter Co-translational protein targeting by the signal recognition particle FEBS Lett. 579 2005 921 926
    • (2005) FEBS Lett. , vol.579 , pp. 921-926
    • Shan, S.-O.1    Walter, P.2
  • 43
    • 77954691102 scopus 로고    scopus 로고
    • In vitro dissection of protein translocation into the mammalian endoplasmic reticulum
    • A. Sharma, M. Mariappan, S. Appathurai, and R.S. Hegde In vitro dissection of protein translocation into the mammalian endoplasmic reticulum Methods Mol. Biol. 619 2010 339 363
    • (2010) Methods Mol. Biol. , vol.619 , pp. 339-363
    • Sharma, A.1    Mariappan, M.2    Appathurai, S.3    Hegde, R.S.4
  • 44
    • 33947218544 scopus 로고    scopus 로고
    • Identification of a targeting factor for posttranslational membrane protein insertion into the ER
    • S. Stefanovic, and R.S. Hegde Identification of a targeting factor for posttranslational membrane protein insertion into the ER Cell 128 2007 1147 1159
    • (2007) Cell , vol.128 , pp. 1147-1159
    • Stefanovic, S.1    Hegde, R.S.2
  • 45
    • 0020994721 scopus 로고
    • Preparation of microsomal membranes for cotranslational protein translocation
    • P. Walter, and G. Blobel Preparation of microsomal membranes for cotranslational protein translocation Methods Enzymol. 96 1983 84 93
    • (1983) Methods Enzymol. , vol.96 , pp. 84-93
    • Walter, P.1    Blobel, G.2
  • 46
    • 0023038665 scopus 로고
    • Import of honeybee prepromellitin into the endoplasmic reticulum. Requirements for membrane insertion, processing, and sequestration
    • R. Zimmermann, and C. Mollay Import of honeybee prepromellitin into the endoplasmic reticulum. Requirements for membrane insertion, processing, and sequestration J. Biol. Chem. 261 1986 12889 12895
    • (1986) J. Biol. Chem. , vol.261 , pp. 12889-12895
    • Zimmermann, R.1    Mollay, C.2
  • 48
    • 54249087710 scopus 로고    scopus 로고
    • Retrotranslocation of prion proteins from the ER by inhibition of GPI signal sequence transamidation
    • Ashok, A.; and Hegde, R.S. (2008). Retrotranslocation of prion proteins from the ER by inhibition of GPI signal sequence transamidation. Mol. Biol. Cell 19, 3463-3476.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3463-3476
    • Ashok, A.1    Hegde, R.S.2
  • 49
    • 0029096050 scopus 로고
    • A posttargeting signal sequence recognition event in the endoplasmic reticulum membrane
    • Jungnickel, B.; and Rapoport, T.A. (1995). A posttargeting signal sequence recognition event in the endoplasmic reticulum membrane. Cell 82, 261-270.
    • (1995) Cell , vol.82 , pp. 261-270
    • Jungnickel, B.1    Rapoport, T.A.2
  • 50
    • 11144255136 scopus 로고    scopus 로고
    • The efficiency of protein compartmentalization into the secretory pathway
    • Levine, C.G.; Mitra, D.; Sharma, A.; Smith, C.L.; and Hegde, R.S. (2005). The efficiency of protein compartmentalization into the secretory pathway. Mol. Biol. Cell 16, 279-291.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 279-291
    • Levine, C.G.1    Mitra, D.2    Sharma, A.3    Smith, C.L.4    Hegde, R.S.5


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