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Volumn 122, Issue 11, 2009, Pages 1768-1777

Dissecting the physiological role of selective transmembrane-segment retention at the ER translocon

Author keywords

Crosslinking; Membrane integration; P2X2 receptor; Sec61

Indexed keywords

MEMBRANE PROTEIN; PROTEIN SEC61; PURINERGIC P2X2 RECEPTOR; TRANSLOCON; UNCLASSIFIED DRUG;

EID: 69449085016     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.046094     Document Type: Article
Times cited : (25)

References (47)
  • 1
    • 15444372454 scopus 로고    scopus 로고
    • Atomic force microscopy imaging demonstrates that P2X2 receptors are trimers but that P2X6 receptor subunits do not oligomerize
    • Barrera, N. P., Ormond, S. J., Henderson, R. M., Murrell-Lagnado, R. D. and Edwardson, J. M. (2005). Atomic force microscopy imaging demonstrates that P2X2 receptors are trimers but that P2X6 receptor subunits do not oligomerize. J. Biol. Chem. 280, 10759-10765.
    • (2005) J. Biol. Chem , vol.280 , pp. 10759-10765
    • Barrera, N.P.1    Ormond, S.J.2    Henderson, R.M.3    Murrell-Lagnado, R.D.4    Edwardson, J.M.5
  • 3
    • 34547650465 scopus 로고    scopus 로고
    • A novel tripartite motif involved in aquaporin topogenesis, monomer folding and tetramerization
    • Buck, T. M., Wagner, J., Grund, S. and Skach, W. R. (2007). A novel tripartite motif involved in aquaporin topogenesis, monomer folding and tetramerization. Nat. Struct. Mol. Biol. 14, 762-769.
    • (2007) Nat. Struct. Mol. Biol , vol.14 , pp. 762-769
    • Buck, T.M.1    Wagner, J.2    Grund, S.3    Skach, W.R.4
  • 4
    • 33846548556 scopus 로고    scopus 로고
    • Biosynthesis of the dystonia-associated AAA+ ATPase torsinA at the endoplasmic reticulum
    • Callan, A. C., Bunning, S., Jones, O. T., High, S. and Swanton, E. (2007). Biosynthesis of the dystonia-associated AAA+ ATPase torsinA at the endoplasmic reticulum. Biochem. J. 401, 607-612.
    • (2007) Biochem. J , vol.401 , pp. 607-612
    • Callan, A.C.1    Bunning, S.2    Jones, O.T.3    High, S.4    Swanton, E.5
  • 5
    • 9444239782 scopus 로고    scopus 로고
    • A misassembled transmembrane domain of a polytopic protein associates with signal peptide peptidase
    • Crawshaw, S. G., Martoglio, B., Meacock, S. L. and High, S. (2004). A misassembled transmembrane domain of a polytopic protein associates with signal peptide peptidase. Biochem. J. 384, 9-17.
    • (2004) Biochem. J , vol.384 , pp. 9-17
    • Crawshaw, S.G.1    Martoglio, B.2    Meacock, S.L.3    High, S.4
  • 6
    • 34247326506 scopus 로고    scopus 로고
    • The oligomeric state of Derlin-1 is modulated by endoplasmic reticulum stress
    • Crawshaw, S. G., Cross, B. C., Wilson, C. M. and High, S. (2007). The oligomeric state of Derlin-1 is modulated by endoplasmic reticulum stress. Mol. Membr. Biol. 24, 113-120.
    • (2007) Mol. Membr. Biol , vol.24 , pp. 113-120
    • Crawshaw, S.G.1    Cross, B.C.2    Wilson, C.M.3    High, S.4
  • 7
    • 69449094517 scopus 로고    scopus 로고
    • Membrane protein biosynthesis at the endoplasmic reticulum
    • ed. R. Zimmermann, Austin, TX: Landes Bioscience
    • Cross, B. C. S. and High, S. (2009). Membrane protein biosynthesis at the endoplasmic reticulum. In Protein Transport Into The Endoplasmic Reticulum (ed. R. Zimmermann). Austin, TX: Landes Bioscience.
    • (2009) Protein Transport Into The Endoplasmic Reticulum
    • Cross, B.C.S.1    High, S.2
  • 8
    • 51049088654 scopus 로고    scopus 로고
    • Control of translocation through the Sec61 translocon by nascent polypeptide structure within the ribosome
    • Daniel, C. J., Conti, B., Johnson, A. E. and Skach, W. R. (2008). Control of translocation through the Sec61 translocon by nascent polypeptide structure within the ribosome. J. Biol. Chem. 283, 20864-20873.
    • (2008) J. Biol. Chem , vol.283 , pp. 20864-20873
    • Daniel, C.J.1    Conti, B.2    Johnson, A.E.3    Skach, W.R.4
  • 9
    • 0342995731 scopus 로고    scopus 로고
    • The cotranslational integration of membrane proteins into the phospholipid bilayer is a multistep process
    • Do, H., Falcone, D., Lin, J., Andrews, D. W. and Johnson, A. E. (1996). The cotranslational integration of membrane proteins into the phospholipid bilayer is a multistep process. Cell 85, 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
  • 10
    • 33846021314 scopus 로고    scopus 로고
    • P2X5 subunit assembly requires scaffolding by the second transmembrane domain and a conserved aspartate
    • Duckwitz, W., Hausmann, R., Aschrafi, A. and Schmalzing, G. (2006). P2X5 subunit assembly requires scaffolding by the second transmembrane domain and a conserved aspartate. J. Biol. Chem. 281, 39561-39572.
    • (2006) J. Biol. Chem , vol.281 , pp. 39561-39572
    • Duckwitz, W.1    Hausmann, R.2    Aschrafi, A.3    Schmalzing, G.4
  • 11
    • 33745188916 scopus 로고    scopus 로고
    • A truncated P2X7 receptor variant (P2X7-j) endogenously expressed in cervical cancer cells antagonizes the full-length P2X7 receptor through hetero-oligomerization
    • Feng, Y. H., Li, X., Wang, L., Zhou, L. and Gorodeski, G. I. (2006). A truncated P2X7 receptor variant (P2X7-j) endogenously expressed in cervical cancer cells antagonizes the full-length P2X7 receptor through hetero-oligomerization. J. Biol. Chem. 281, 17228-17237.
    • (2006) J. Biol. Chem , vol.281 , pp. 17228-17237
    • Feng, Y.H.1    Li, X.2    Wang, L.3    Zhou, L.4    Gorodeski, G.I.5
  • 12
    • 0020039866 scopus 로고
    • Isolation of intracellular membranes by means of sodium carbonate treatment: Application to endoplasmic reticulum
    • Fujiki, Y., Hubbard, A. L., Fowler, S. and Lazarow, P. B. (1982). Isolation of intracellular membranes by means of sodium carbonate treatment: Application to endoplasmic reticulum. J. Cell Biol. 93, 97-102.
    • (1982) J. Cell Biol , vol.93 , pp. 97-102
    • Fujiki, Y.1    Hubbard, A.L.2    Fowler, S.3    Lazarow, P.B.4
  • 13
    • 22444450987 scopus 로고    scopus 로고
    • A substrate-specific inhibitor of protein translocation into the endoplasmic reticulum
    • Garrison, J. L., Kunkel, E. J., Hegde, R. S. and Taunton, J. (2005). A substrate-specific inhibitor of protein translocation into the endoplasmic reticulum. Nature 436, 285-289.
    • (2005) Nature , vol.436 , pp. 285-289
    • Garrison, J.L.1    Kunkel, E.J.2    Hegde, R.S.3    Taunton, J.4
  • 14
    • 0026038363 scopus 로고
    • Transcription of full-length and truncated mRNA transcripts to study protein translocation across the endoplasmic reticulum
    • Gilmore, R., Collins, P., Johnson, J., Kellaris, K. and Rapiejko, P. (1991). Transcription of full-length and truncated mRNA transcripts to study protein translocation across the endoplasmic reticulum. Methods Cell Biol. 34, 223-239.
    • (1991) Methods Cell Biol , vol.34 , pp. 223-239
    • Gilmore, R.1    Collins, P.2    Johnson, J.3    Kellaris, K.4    Rapiejko, P.5
  • 15
    • 48249151759 scopus 로고    scopus 로고
    • The concept of translocational regulation
    • Hegde, R. S. and Kang, S. W. (2008). The concept of translocational regulation. J. Cell Biol. 182, 225-232.
    • (2008) J. Cell Biol , vol.182 , pp. 225-232
    • Hegde, R.S.1    Kang, S.W.2
  • 16
    • 0042815085 scopus 로고    scopus 로고
    • Cooperation of transmembrane segments during the integration of a double-spanning protein into the ER membrane
    • Heinrich, S. U. and Rapoport, T. A. (2003). Cooperation of transmembrane segments during the integration of a double-spanning protein into the ER membrane. EMBO J. 22, 3654-3663.
    • (2003) EMBO J , vol.22 , pp. 3654-3663
    • Heinrich, S.U.1    Rapoport, T.A.2
  • 17
    • 0034697967 scopus 로고    scopus 로고
    • The Sec61p complex mediates the integration of a membrane protein by allowing lipid partitioning of the transmembrane domain
    • Heinrich, S. U., Mothes, W., Brunner, J. and Rapoport, T. A. (2000). The Sec61p complex mediates the integration of a membrane protein by allowing lipid partitioning of the transmembrane domain. Cell 102, 233-244.
    • (2000) Cell , vol.102 , pp. 233-244
    • Heinrich, S.U.1    Mothes, W.2    Brunner, J.3    Rapoport, T.A.4
  • 19
    • 33746923016 scopus 로고    scopus 로고
    • Active and passive displacement of transmembrane domains both occur during opsin biogenesis at the Sec61 translocon
    • Ismail, N., Crawshaw, S. G. and High, S. (2006). Active and passive displacement of transmembrane domains both occur during opsin biogenesis at the Sec61 translocon. J. Cell Sci. 119, 2826-2836.
    • (2006) J. Cell Sci , vol.119 , pp. 2826-2836
    • Ismail, N.1    Crawshaw, S.G.2    High, S.3
  • 20
    • 42449130051 scopus 로고    scopus 로고
    • Specific transmembrane segments are selectively delayed at the ER translocon during opsin biogenesis
    • Ismail, N., Crawshaw, S. G., Cross, B. C., Haagsma, A. C. and High, S. (2008). Specific transmembrane segments are selectively delayed at the ER translocon during opsin biogenesis. Biochem. J. 411, 495-506.
    • (2008) Biochem. J , vol.411 , pp. 495-506
    • Ismail, N.1    Crawshaw, S.G.2    Cross, B.C.3    Haagsma, A.C.4    High, S.5
  • 21
    • 0035805612 scopus 로고    scopus 로고
    • Amino acid residues involved in gating identified in the first membrane-spanning domain of the rat P2X(2) receptor
    • Jiang, L. H., Rassendren, F., Spelta, V., Surprenant, A. and North, R. A. (2001). Amino acid residues involved in gating identified in the first membrane-spanning domain of the rat P2X(2) receptor. J. Biol. Chem. 276, 14902-14908.
    • (2001) J. Biol. Chem , vol.276 , pp. 14902-14908
    • Jiang, L.H.1    Rassendren, F.2    Spelta, V.3    Surprenant, A.4    North, R.A.5
  • 23
    • 0031781639 scopus 로고    scopus 로고
    • The beta subunit of the Sec61 complex facilitates cotranslational protein transport and interacts with the signal peptidase during translocation
    • Kalies, K. U., Rapoport, T. A. and Hartmann, E. (1998). The beta subunit of the Sec61 complex facilitates cotranslational protein transport and interacts with the signal peptidase during translocation. J. Cell Biol. 141, 887-894.
    • (1998) J. Cell Biol , vol.141 , pp. 887-894
    • Kalies, K.U.1    Rapoport, T.A.2    Hartmann, E.3
  • 24
    • 25144519777 scopus 로고    scopus 로고
    • Translocation of a long amino-terminal domain through ER membrane by following signal-anchor sequence
    • Kida, Y., Mihara, K. and Sakaguchi, M. (2005). Translocation of a long amino-terminal domain through ER membrane by following signal-anchor sequence. EMBO J. 24, 3202-3213.
    • (2005) EMBO J , vol.24 , pp. 3202-3213
    • Kida, Y.1    Mihara, K.2    Sakaguchi, M.3
  • 25
    • 0036810271 scopus 로고    scopus 로고
    • Protein folding during cotranslational translocation in the endoplasmic reticulum
    • Kowarik, M., Kung, S., Martoglio, B. and Helenius, A. (2002). Protein folding during cotranslational translocation in the endoplasmic reticulum. Mol. Cell 10, 769-778.
    • (2002) Mol. Cell , vol.10 , pp. 769-778
    • Kowarik, M.1    Kung, S.2    Martoglio, B.3    Helenius, A.4
  • 26
    • 0029960038 scopus 로고    scopus 로고
    • Reinitiation of protein translocation across the endoplasmic reticulum membrane for the topogenesis of multispanning membrane proteins
    • Kuroiwa, T., Sakaguchi, M., Omura, T. and Mihara, K. (1996). Reinitiation of protein translocation across the endoplasmic reticulum membrane for the topogenesis of multispanning membrane proteins. J. Biol. Chem. 271, 6423-6428.
    • (1996) J. Biol. Chem , vol.271 , pp. 6423-6428
    • Kuroiwa, T.1    Sakaguchi, M.2    Omura, T.3    Mihara, K.4
  • 27
    • 0031030059 scopus 로고    scopus 로고
    • Discrete cross-linking products identified during membrane protein biosynthesis
    • Laird, V. and High, S. (1997). Discrete cross-linking products identified during membrane protein biosynthesis. J. Biol. Chem. 272, 1983-1989.
    • (1997) J. Biol. Chem , vol.272 , pp. 1983-1989
    • Laird, V.1    High, S.2
  • 28
    • 0028900576 scopus 로고
    • A novel integration signal that is composed of two transmembrane segments is required to integrate the Neurospora plasma membrane H(+)-ATPase into microsomes
    • Lin, J. and Addison, R. (1995). A novel integration signal that is composed of two transmembrane segments is required to integrate the Neurospora plasma membrane H(+)-ATPase into microsomes. J. Biol. Chem. 270, 6935-6941.
    • (1995) J. Biol. Chem , vol.270 , pp. 6935-6941
    • Lin, J.1    Addison, R.2
  • 29
    • 0029002962 scopus 로고
    • The protein-conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer
    • Martoglio, B., Hofmann, M. W., Brunner, J. and Dobberstein, B. (1995). The protein-conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer. Cell 81, 207-214.
    • (1995) Cell , vol.81 , pp. 207-214
    • Martoglio, B.1    Hofmann, M.W.2    Brunner, J.3    Dobberstein, B.4
  • 30
    • 0141992130 scopus 로고    scopus 로고
    • Cotranslational protein integration into the ER membrane is mediated by the binding of nascent chains to translocon proteins
    • McCormick, P. J., Miao, Y., Shao, Y., Lin, J. and Johnson, A. E. (2003). Cotranslational protein integration into the ER membrane is mediated by the binding of nascent chains to translocon proteins. Mol. Cell 12, 329-341.
    • (2003) Mol. Cell , vol.12 , pp. 329-341
    • McCormick, P.J.1    Miao, Y.2    Shao, Y.3    Lin, J.4    Johnson, A.E.5
  • 31
    • 0036906637 scopus 로고    scopus 로고
    • Different transmembrane domains associate with distinct endoplasmic reticulum components during membrane integration of a polytopic protein
    • Meacock, S. L., Lecomte, F. J., Crawshaw, S. G. and High, S. (2002). Different transmembrane domains associate with distinct endoplasmic reticulum components during membrane integration of a polytopic protein. Mol. Biol. Cell 13, 4114-4129.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 4114-4129
    • Meacock, S.L.1    Lecomte, F.J.2    Crawshaw, S.G.3    High, S.4
  • 32
    • 33750498869 scopus 로고    scopus 로고
    • Asn- and Asp-mediated interactions between transmembrane helices during translocon-mediated membrane protein assembly
    • Meindl-Beinker, N. M., Lundin, C., Nilsson, I., White, S. H. and von Heijne, G. (2006). Asn- and Asp-mediated interactions between transmembrane helices during translocon-mediated membrane protein assembly. EMBO Rep. 7, 1111-1116.
    • (2006) EMBO Rep , vol.7 , pp. 1111-1116
    • Meindl-Beinker, N.M.1    Lundin, C.2    Nilsson, I.3    White, S.H.4    von Heijne, G.5
  • 33
  • 34
    • 42949166161 scopus 로고    scopus 로고
    • Assembly and trafficking of P2X purinergic receptors (Review)
    • Murrell-Lagnado, R. D. and Qureshi, O. S. (2008). Assembly and trafficking of P2X purinergic receptors (Review). Mol. Membr. Biol. 25, 321-331.
    • (2008) Mol. Membr. Biol , vol.25 , pp. 321-331
    • Murrell-Lagnado, R.D.1    Qureshi, O.S.2
  • 35
    • 0036788971 scopus 로고    scopus 로고
    • Molecular physiology of P2X receptors
    • North, R. A. (2002). Molecular physiology of P2X receptors. Physiol. Rev. 82, 1013-1067.
    • (2002) Physiol. Rev , vol.82 , pp. 1013-1067
    • North, R.A.1
  • 37
    • 49549087761 scopus 로고    scopus 로고
    • MINS2: Revisiting the molecular code for transmembrane-helix recognition by the Sec61 translocon
    • Park, Y. and Helms, V. (2008). MINS2: revisiting the molecular code for transmembrane-helix recognition by the Sec61 translocon. Bioinformatics 24, 1819-1820.
    • (2008) Bioinformatics , vol.24 , pp. 1819-1820
    • Park, Y.1    Helms, V.2
  • 38
    • 61949084073 scopus 로고    scopus 로고
    • Sequence-specific retention and regulated integration of a nascent membrane protein by the ER Sec61 translocon
    • Pitonzo, D., Yang, Z., Matsumura, Y., Johnson, A. E. and Skach, W. R. (2009). Sequence-specific retention and regulated integration of a nascent membrane protein by the ER Sec61 translocon. Mol. Biol. Cell 20, 685-698.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 685-698
    • Pitonzo, D.1    Yang, Z.2    Matsumura, Y.3    Johnson, A.E.4    Skach, W.R.5
  • 39
    • 18844387083 scopus 로고    scopus 로고
    • Signal recognition particles in chloroplasts, bacteria, yeast and mammals (review)
    • Pool, M. R. (2005). Signal recognition particles in chloroplasts, bacteria, yeast and mammals (review). Mol. Membr. Biol. 22, 3-15.
    • (2005) Mol. Membr. Biol , vol.22 , pp. 3-15
    • Pool, M.R.1
  • 40
    • 36749001066 scopus 로고    scopus 로고
    • Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes
    • Rapoport, T. A. (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
  • 41
    • 17744395499 scopus 로고    scopus 로고
    • Biogenesis of CFTR and other polytopic membrane proteins: New roles for the ribosome-translocon complex
    • Sadlish, H. and Skach, W. R. (2004). Biogenesis of CFTR and other polytopic membrane proteins: new roles for the ribosome-translocon complex. J. Membr. Biol. 202, 115-126.
    • (2004) J. Membr. Biol , vol.202 , pp. 115-126
    • Sadlish, H.1    Skach, W.R.2
  • 42
    • 27144549973 scopus 로고    scopus 로고
    • Sequential triage of transmembrane segments by Sec61alpha during biogenesis of a native multispanning membrane protein
    • Sadlish, H., Pitonzo, D., Johnson, A. E. and Skach, W. R. (2005). Sequential triage of transmembrane segments by Sec61alpha during biogenesis of a native multispanning membrane protein. Nat. Struct. Mol. Biol. 12, 870-878.
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 870-878
    • Sadlish, H.1    Pitonzo, D.2    Johnson, A.E.3    Skach, W.R.4
  • 43
    • 21844442598 scopus 로고    scopus 로고
    • Double-spanning plant viral movement protein integration into the endoplasmic reticulum membrane is signal recognition particle-dependent, translocon-mediated, and concerted
    • Sauri, A., Saksena, S., Salgado, J., Johnson, A. E. and Mingarro, I. (2005). Double-spanning plant viral movement protein integration into the endoplasmic reticulum membrane is signal recognition particle-dependent, translocon-mediated, and concerted. J. Biol. Chem. 280, 25907-25912.
    • (2005) J. Biol. Chem , vol.280 , pp. 25907-25912
    • Sauri, A.1    Saksena, S.2    Salgado, J.3    Johnson, A.E.4    Mingarro, I.5
  • 44
    • 0027519416 scopus 로고
    • Amino-terminal assembly of human P-glycoprotein at the endoplasmic reticulum is directed by cooperative actions of two internal sequences
    • Skach, W. R. and Lingappa, V. R. (1993). Amino-terminal assembly of human P-glycoprotein at the endoplasmic reticulum is directed by cooperative actions of two internal sequences. J. Biol. Chem. 268, 23552-23561.
    • (1993) J. Biol. Chem , vol.268 , pp. 23552-23561
    • Skach, W.R.1    Lingappa, V.R.2
  • 46
    • 48249095616 scopus 로고    scopus 로고
    • How translocons select transmembrane helices
    • White, S. H. and von Heijne, G. (2008). How translocons select transmembrane helices. Annu. Rev. Biophys. 37, 23-42.
    • (2008) Annu. Rev. Biophys , vol.37 , pp. 23-42
    • White, S.H.1    von Heijne, G.2
  • 47
    • 34347249218 scopus 로고    scopus 로고
    • Contribution of hydrophobic and electrostatic interactions to the membrane integration of the Shaker K+ channel voltage sensor domain
    • Zhang, L., Sato, Y., Hessa, T., von Heijne, G., Lee, J. K., Kodama, I., Sakaguchi, M. and Uozumi, N. (2007). Contribution of hydrophobic and electrostatic interactions to the membrane integration of the Shaker K+ channel voltage sensor domain. Proc. Natl. Acad. Sci. USA 104, 8263-8268.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 8263-8268
    • Zhang, L.1    Sato, Y.2    Hessa, T.3    von Heijne, G.4    Lee, J.K.5    Kodama, I.6    Sakaguchi, M.7    Uozumi, N.8


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