Cited by 460Cellular transport and secretionRNA and protein synthesis mechanismsNuclear Structure and Function

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Protein Translocation Across Biological Membranes

Wickner, William, Schekman, Randy·2005·Science

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Abstract

Subcellular compartments have unique protein compositions, yet protein synthesis only occurs in the cytosol and in mitochondria and chloroplasts. How do proteins get where they need to go? The first steps are targeting to an organelle and efficient translocation across its limiting membrane. Given that most transport systems are exquisitely substrate specific, how are diverse protein sequences recognized for translocation? Are they translocated as linear polypeptide chains or after folding? During translocation, how are diverse amino acyl side chains accommodated? What are the proteins and the lipid environment that catalyze transport and couple it to energy? How is translocation coordinated with protein synthesis and folding, and how are partially translocated transmembrane proteins released into the lipid bilayer? We review here the marked progress of the past 35 years and salient questions for future work. Subcellular compartments have unique protein compositions, yet protein synthesis only occurs in the cytosol and in mitochondria and chloroplasts. How do proteins get where they need to go? The first steps are targeting to an organelle and efficient translocation across its limiting membrane. Given that most transport systems are exquisitely substrate specific, how are diverse protein sequences recognized for translocation? Are they translocated as linear polypeptide chains or after folding? During translocation, how are diverse amino acyl side chains accommodated? What are the proteins and the lipid environment that catalyze transport and couple it to energy? How is translocation coordinated with protein synthesis and folding, and how are partially translocated transmembrane proteins released into the lipid bilayer? We review here the marked progress of the past 35 years and salient questions for future work.

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X-ray structure of a protein-conducting channel
van den Berg, B., Clemons, W., Collinson, I. R., Modis, Y., Hartmann, E., Harrison, S. C., & Rapoport, T. A. (2003) · Nature · doi:10.1038/nature02218 · Cited by 1,236
ERAD: the long road to destruction
Meusser, B., Hirsch, C., Jarosch, E., & Sommer, T. (2005) · Nature Cell Biology · doi:10.1038/ncb0805-766 · Cited by 1,221
Transfer of proteins across membranes. II. Reconstitution of functional rough microsomes from heterologous components.
Blobel, G., & Dobberstein, B. (1975) · The Journal of Cell Biology · doi:10.1083/jcb.67.3.852 · Cited by 1,173
A conserved tripeptide sorts proteins to peroxisomes.
Gould, S. J., Keller, G. A., Hosken, N. A., Wilkinson, J. Q., & Subramani, S. E. (1989) · The Journal of Cell Biology · doi:10.1083/jcb.108.5.1657 · Cited by 1,107
A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol
Ye, Y., Shibata, Y., Yun, C., Ron, D., & Rapoport, T. A. (2004) · Nature · doi:10.1038/nature02656 · Cited by 963
Translocation of proteins across the endoplasmic reticulum III. Signal recognition protein (SRP) causes signal sequence-dependent and site-specific arrest of chain elongation that is released by microsomal membranes.
Walter, P., & Blobel, G. (1981) · The Journal of Cell Biology · doi:10.1083/jcb.91.2.557 · Cited by 810
Signal recognition particle contains a 7S RNA essential for protein translocation across the endoplasmic reticulum
Walter, P., & Blobel, G. (1982) · Nature · doi:10.1038/299691a0 · Cited by 779
Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria
Eilers, M., & Schatz, G. (1986) · Nature · doi:10.1038/322228a0 · Cited by 725
ER Degradation of a Misfolded Luminal Protein by the Cytosolic Ubiquitin-Proteasome Pathway
Hiller, M. M., Finger, A., Schweiger, M. W., & Wolf, D. H. (1996) · Science · doi:10.1126/science.273.5282.1725 · Cited by 706
A common export pathway for proteins binding complex redox cofactors?
Berks, B. C. (1996) · Molecular Microbiology · doi:10.1046/j.1365-2958.1996.00114.x · Cited by 685
A membrane protein required for dislocation of misfolded proteins from the ER
Lilley, B. N., & Ploegh, H. L. (2004) · Nature · doi:10.1038/nature02592 · Cited by 674
Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane
Görlich, D. (1993) · Cell · doi:10.1016/0092-8674(93)90483-7 · Cited by 658
A Possible Precursor of Immunoglobulin Light Chains
Milstein, C., Brownlee, G. G., Harrison, T. M., & Mathews, M. B. (1972) · Nature New Biology · doi:10.1038/newbio239117a0 · Cited by 603
The binding cascade of SecB to SecA to SecYE mediates preprotein targeting to the E. coli plasma membrane
Hartl, F.-U., Lecker, S., Schiebel, E., Hendrick, J. P., & Wickner, W. (1990) · Cell · doi:10.1016/0092-8674(90)90160-g · Cited by 562
Self-citation
Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation
Plemper, R. K., Böhmler, S., Bordallo, J., Sommer, T., & Wolf, D. H. (1997) · Nature · doi:10.1038/42276 · Cited by 555
Synchronised transmembrane insertion and glycosylation of a nascent membrane protein
Rothman, J. E., & Lodish, H. F. (1977) · Nature · doi:10.1038/269775a0 · Cited by 531
Purification of a membrane-associated protein complex required for protein translocation across the endoplasmic reticulum.
Walter, P., & Blobel, G. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.12.7112 · Cited by 513
The purified E. coli integral membrane protein is sufficient for reconstitution of SecA-dependent precursor protein translocation
Brundage, L., Hendrick, J. P., Schiebel, E., Driessen, A. J. M., & Wickner, W. (1990) · Cell · doi:10.1016/0092-8674(90)90111-q · Cited by 505
Self-citation
E. coli mutant pleiotropically defective in the export of secreted proteins
Oliver, D. B., & Beckwith, J. (1981) · Cell · doi:10.1016/0092-8674(81)90184-7 · Cited by 503
Protein Disulfide Isomerase Acts as a Redox-Dependent Chaperone to Unfold Cholera Toxin
Tsai, B., Rodighiero, C., Lencer, W. I., & Rapoport, T. A. (2001) · Cell · doi:10.1016/s0092-8674(01)00289-6 · Cited by 484
Protein translocation across the endoplasmic reticulum. II. Isolation and characterization of the signal recognition particle receptor.
Gilmore, R., Walter, P., & Blobel, G. (1982) · The Journal of Cell Biology · doi:10.1083/jcb.95.2.470 · Cited by 479
Role of EDEM in the Release of Misfolded Glycoproteins from the Calnexin Cycle
Molinari, M., Calanca, V., Galli, C., Lucca, P., & Paganetti, P. (2003) · Science · doi:10.1126/science.1079474 · Cited by 470
Contribution of the Endoplasmic Reticulum to Peroxisome Formation
Hoepfner, D., Schildknegt, D., Braakman, I., Philippsen, P., & Tabak, H. F. (2005) · Cell · doi:10.1016/j.cell.2005.04.025 · Cited by 463
Import of proteins into mitochondria: precursor forms of the extramitochondrially made F1-ATPase subunits in yeast.
Maccecchini, M. L., Rudin, Y., Blobel, G., & Schatz, G. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.1.343 · Cited by 453
EDEM As an Acceptor of Terminally Misfolded Glycoproteins Released from Calnexin
Oda, Y., Hosokawa, N., Wada, I., & Nagata, K. (2003) · Science · doi:10.1126/science.1079181 · Cited by 453
BiP Acts as a Molecular Ratchet during Posttranslational Transport of Prepro-α Factor across the ER Membrane
Matlack, K. E. S., Misselwitz, B., Plath, K., & Rapoport, T. A. (1999) · Cell · doi:10.1016/s0092-8674(00)80767-9 · Cited by 447
Evolutionary conservation of biogenesis of β-barrel membrane proteins
Paschen, S. A., Waizenegger, T., Stan, T., Preuss, M., Cyrklaff, M., Hell, K., Rapaport, D., & Neupert, W. (2003) · Nature · doi:10.1038/nature02208 · Cited by 431
A yeast mutant defective at an early stage in import of secretory protein precursors into the endoplasmic reticulum.
Deshaies, R. J., & Schekman, R. W. (1987) · The Journal of Cell Biology · doi:10.1083/jcb.105.2.633 · Cited by 425
Self-citation
Machinery for protein sorting and assembly in the mitochondrial outer membrane
Wiedemann, N., Kozjak‐Pavlovic, V., Chacińska, A., Schönfisch, B., Rospert, S., Ryan, M. T., Pfanner, N., & Meisinger, C. (2003) · Nature · doi:10.1038/nature01753 · Cited by 415
Assembly of ER-associated protein degradation in vitro: dependence on cytosol, calnexin, and ATP.
McCracken, A. A., & Brodsky, J. L. (1996) · The Journal of Cell Biology · doi:10.1083/jcb.132.3.291 · Cited by 409
Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation
Pilon, M., Schekman, R., & Römisch, K. (1997) · The EMBO Journal · doi:10.1093/emboj/16.15.4540 · Cited by 406
Self-citation
SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coli.
Lill, R., Cunningham, K. W., Brundage, L., Ito, K., Oliver, D. B., & Wickner, W. T. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb03458.x · Cited by 401
Self-citation
The Preprotein Translocation Channel of the Outer Membrane of Mitochondria
Künkele, K., Heins, S., Dembowski, M., Nargang, F. E., Benz, R., Thieffry, M., Walz, J. C., Lill, R., Nußberger, S., & Neupert, W. (1998) · Cell · doi:10.1016/s0092-8674(00)81206-4 · Cited by 397
The protein import motor of mitochondria
Neupert, W., & Brunner, M. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm878 · Cited by 394
Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p
Panzner, S., Dreier, L., Hartmann, E., Kostka, S., & Rapoport, T. A. (1995) · Cell · doi:10.1016/0092-8674(95)90077-2 · Cited by 393
Der1, a novel protein specifically required for endoplasmic reticulum degradation in yeast.
Knop, M., Finger, A. C., Braun, T., Hellmuth, K., & Wolf, D. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00411.x · Cited by 388
Post-translational transport into intact chloroplasts of a precursor to the small subunit of ribulose-1,5-bisphosphate carboxylase
Chua, N., & Schmidt, G. W. (1978) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.75.12.6110 · Cited by 384
Suppressor mutations that restore export of a protein with a defective signal sequence
Emr, S. D., Hanley-Way, S., & Silhavy, T. J. (1981) · Cell · doi:10.1016/0092-8674(81)90272-5 · Cited by 382
Biosynthesis of Serum Proteins and Ferritin by Free and Attached Ribosomes of Rat Liver
Redman, C. M. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94321-8 · Cited by 362
Import of carrier proteins into the mitochondrial inner membrane mediated by Tim22
Sirrenberg, C., Bauer, M. F., Guiard, B., Neupert, W., & Brunner, M. (1996) · Nature · doi:10.1038/384582a0 · Cited by 342
An oligomeric protein is imported into peroxisomes in vivo.
McNew, J. A., & Goodman, J. M. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.127.5.1245 · Cited by 339
The Protein Import Machinery of Mitochondria
Wiedemann, N., Frazier, A. E., & Pfanner, N. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.r400003200 · Cited by 336
A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum
Sommer, T., & Jentsch, S. (1993) · Nature · doi:10.1038/365176a0 · Cited by 334
In vitro protein translocation across the yeast endoplasmic reticulum: ATP-dependent post-translational translocation of the prepro-α-factor
Hansen, W., García, P. D., & Walter, P. (1986) · Cell · doi:10.1016/0092-8674(86)90325-9 · Cited by 333
The E. coli signal recognition particle is required for the insertion of a subset of inner membrane proteins.
Ulbrandt, N. D., Newitt, J. A., & Bernstein, H. D. (1997) · Cell · doi:10.1016/s0092-8674(00)81839-5 · Cited by 332
Peroxisome Biogenesis
Purdue, P. E., & Lazarow, P. B. (2001) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.17.1.701 · Cited by 323
CONTROLLED PROTEOLYSIS OF NASCENT POLYPEPTIDES IN RAT LIVER CELL FRACTIONS
Sabatini, D. D., & Blobel, G. (1970) · The Journal of Cell Biology · doi:10.1083/jcb.45.1.146 · Cited by 317
Preferential Synthesis of Ferritin and Albumin by Different Populations of Liver Polysomes
Hicks, S. J., Drysdale, J., & Munro, H. N. (1969) · Science · doi:10.1126/science.164.3879.584 · Cited by 300
The signal recognition particle in S. cerevisiae
Hann, B. C., & Walter, P. (1991) · Cell · doi:10.1016/0092-8674(91)90577-l · Cited by 298
SecA membrane cycling at SecYEG is driven by distinct ATP binding and hydrolysis events and is regulated by SecD and SecF
Economou, A., Pogliano, J., Beckwith, J. R., Oliver, D. B., & Wickner, W. T. (1995) · Cell · doi:10.1016/0092-8674(95)90143-4 · Cited by 294
Self-citation
The TatA component of the twin-arginine protein transport system forms channel complexes of variable diameter
Gohlke, U., Pullan, L., McDevitt, C. A., Porcelli, I., de Leeuw, E., Palmer, T., Saibil, H. R., & Berks, B. C. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0503558102 · Cited by 277
Import of stably folded proteins into peroxisomes.
Walton, P. A., Hill, P. E., & Subramani, S. E. (1995) · Molecular Biology of the Cell · doi:10.1091/mbc.6.6.675 · Cited by 275
The E. coli ffh gene is necessary for viability and efficient protein export
Phillips, G. J., & Silhavy, T. J. (1992) · Nature · doi:10.1038/359744a0 · Cited by 269
Co-translocation of a Periplasmic Enzyme Complex by a Hitchhiker Mechanism through the Bacterial Tat Pathway
Rodrigue, A., Chanal, A., Beck, K., Müller, M. P., & Wu, L. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.19.13223 · Cited by 268
GENETICS AND BIOGENESIS OF CHLOROPLASTS AND MITOCHONDRIA
Neupert, W., Sebald, W., & Werner, S. (1976) · Cited by 262
SRP-mediated protein targeting: structure and function revisited
Luirink, J. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.03.013 · Cited by 254
Htm1p, a mannosidase‐like protein, is involved in glycoprotein degradation in yeast
Jakob, C. A., Bodmer, D., Spirig, U., Bättig, P., Marcil, A., Dignard, D., Bergeron, J. J. M., Thomas, D. Y., & Aebi, M. (2001) · The EMBO Reports · doi:10.1093/embo-reports/kve089 · Cited by 252
Each of the activities of signal recognition particle (SRP) is contained within a distinct domain: Analysis of biochemical mutants of SRP
Siegel, V. (1988) · Cell · doi:10.1016/0092-8674(88)90529-6 · Cited by 248
Vectorial discharge of peptides released by puromycin from attached ribosomes.
Redman, C. M., & Sabatini, D. D. (1966) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.56.2.608 · Cited by 243
The pas8 mutant of Pichia pastoris exhibits the peroxisomal protein import deficiencies of Zellweger syndrome cells--the PAS8 protein binds to the COOH-terminal tripeptide peroxisomal targeting signal, and is a member of the TPR protein family [published erratum appears in J Cell Biol 1993 Sep;122(5):following 1143]
McCollum, D. (1993) · The Journal of Cell Biology · doi:10.1083/jcb.121.4.761 · Cited by 243
The Human Peroxisomal Targeting Signal Receptor, Pex5p, Is Translocated into the Peroxisomal Matrix and Recycled to the Cytosol
Dammai, V., & Subramani, S. E. (2001) · Cell · doi:10.1016/s0092-8674(01)00310-5 · Cited by 241
Translocation of domains of nascent periplasmic proteins across the cytoplasmic membrane is independent of elongation.
Randall, L. L. (1983) · Cell · doi:10.1016/0092-8674(83)90352-5 · Cited by 234
Inversion of the Membrane Topology of SecG Coupled with SecA-Dependent Preprotein Translocation
Nishiyama, K., Suzuki, T., & Tokuda, H. (1996) · Cell · doi:10.1016/s0092-8674(00)81083-1 · Cited by 218
Escherichia coli YidC is a membrane insertase for Sec-independent proteins.
Serek, J., Bauer‐Manz, G., Struhalla, G., van den Berg, L., Kiefer, D., Dalbey, R., & Kuhn, A. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600063 · Cited by 211
British Optical Astronomy
Burbidge, G. R. (1972) · Nature · doi:10.1038/239117a0 · Cited by 204
Reciprocal stimulation of GTP hydrolysis by two directly interacting GTPases
Powers, T., & Walter, P. (1995) · Science · doi:10.1126/science.7660124 · Cited by 203
A novel signal recognition particle targets light-harvesting proteins to the thylakoid membranes
Schünemann, D., Gupta, S., Cartieaux, F., Klimyuk, V. I., Jones, J. D. G., Nussaume, L., & Hoffman, N. E. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.17.10312 · Cited by 200
Removal of the Alu structural domain from signal recognition particle leaves its protein translocation activity intact
Siegel, V., & Walter, P. (1986) · Nature · doi:10.1038/320081a0 · Cited by 179
Synthesis and assembly of the membrane proteins in E. coli
Ito, K., Sato, T., & Yura, T. (1977) · Cell · doi:10.1016/0092-8674(77)90073-3 · Cited by 179
In vitro translocation of bacterial proteins across the plasma membrane of Escherichia coli.
Müller, M. P., & Blobel, G. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.23.7421 · Cited by 174
Mechanisms of Protein Import and Routing in Chloroplasts
Jarvis, P., & Robinson, C. (2004) · Current Biology · doi:10.1016/j.cub.2004.11.049 · Cited by 174
Insertion into the mitochondrial inner membrane of a polytopic protein, the nuclear‐encoded Oxa1p
Herrmann, J. M., Neupert, W., & Stuart, R. A. (1997) · The EMBO Journal · doi:10.1093/emboj/16.9.2217 · Cited by 172
ATP is essential for protein translocation into Escherichia coli membrane vesicles.
Chen, L., & Tai, P. C. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.13.4384 · Cited by 164
Disulfide bridge formation between SecY and a translocating polypeptide localizes the translocation pore to the center of SecY
Cannon, K. S., Or, E., Clemons, W., Shibata, Y., & Rapoport, T. A. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200412019 · Cited by 164
A signal sequence is not sufficient to lead β-galactosidase out of the cytoplasm
Moreno, F., Fowler, A. V., Hall, M. N., Silhavy, T. J., Zabin, I., & Schwartz, M. (1980) · Nature · doi:10.1038/286356a0 · Cited by 149
Interplay of signal recognition particle and trigger factor at L23 near the nascent chain exit site on theEscherichia coliribosome
Ullers, R. S., Houben, E. N. G., Raine, A., ten Hagen‐Jongman, C. M., Ehrenberg, M., Brunner, J., Oudega, B., Harms, N., & Luirink, J. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200302130 · Cited by 142
In vitro SYNTHESIS OF DIFFERENT CATEGORIES OF SPECIFIC PROTEIN BY MEMBRANE-BOUND AND FREE RIBOSOMES
GANOZA, M. C., & Williams, C. A. (1969) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.63.4.1370 · Cited by 141
Identification and characterization of a membrane component essential for the translocation of nascent proteins across the membrane of the endoplasmic reticulum.
Meyer, D. I., & Dobberstein, B. (1980) · The Journal of Cell Biology · doi:10.1083/jcb.87.2.503 · Cited by 139
Empty Site Forms of the SRP54 and SRα GTPases Mediate Targeting of Ribosome–Nascent Chain Complexes to the Endoplasmic Reticulum
Rapiejko, P. J., & Gilmore, R. (1997) · Cell · doi:10.1016/s0092-8674(00)80253-6 · Cited by 134
Escherichia coli mutants accumulating the precursor of a secreted protein in the cytoplasm
Bassford, P. J., & Beckwith, J. (1979) · Nature · doi:10.1038/277538a0 · Cited by 132
Binding, activation and dissociation of the dimeric SecA ATPase at the dimeric SecYEG translocase
Duong, F. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg418 · Cited by 132
Stepwise Movement of Preproteins in the Process of Translocation across the Cytoplasmic Membrane of Escherichia coli
Uchida, K., Mori, H., & Mizushima, S. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.52.30862 · Cited by 127
Transport of Cytoplasmically Synthesized Proteins into the Mitochondria in a Cell Free System from Neurospora crassa
Harmey, M. A., Hallermayer, G., Korb, H., & Neupert, W. (1977) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1977.tb11979.x · Cited by 120
Uncoupling retro‐translocation and degradation in the ER‐associated degradation of a soluble protein
Lee, R. J., Liu, C., Harty, C., McCracken, A. A., Latterich, M., Römisch, K., Demartino, G., Thomas, P., & Brodsky, J. L. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600232 · Cited by 113
Peroxisomal Membrane Fusion Requires Two Aaa Family Atpases, Pex1p and Pex6p
Titorenko, V. I., & Rachubinski, R. A. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.150.4.881 · Cited by 113
The protein translocation channel binds proteasomes to the endoplasmic reticulum membrane
Kalies, K., Allan, S., Sergeyenko, T. V., Kröger, H., & Römisch, K. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600731 · Cited by 111
Energetics of Protein Transport across Biological Membranes
Alder, N. N., & Theg, S. M. (2003) · Cell · doi:10.1016/s0092-8674(03)00032-1 · Cited by 109
Signal recognition particle receptor is important for cell growth and protein secretion in Saccharomyces cerevisiae.
Ogg, S. C., Poritz, M. A., & Walter, P. (1992) · Molecular Biology of the Cell · doi:10.1091/mbc.3.8.895 · Cited by 107
Bacterial leader peptidase, a membrane protein without a leader peptide, uses the same export pathway as pre-secretory proteins
Wolfe, P. B., & Wickner, W. T. (1984) · Cell · doi:10.1016/0092-8674(84)90056-4 · Cited by 82
Self-citation
In vivo and in vitro analysis of ptl1, a yeast ts mutant with a membrane‐associated defect in protein translocation.
Toyn, J. H., Hibbs, A. R., Sanz, P., Crowe, J., & Meyer, D. I. (1988) · The EMBO Journal · doi:10.1002/j.1460-2075.1988.tb03333.x · Cited by 77
Evaluating the oligomeric state of SecYEG in preprotein translocase
Yahr, T. L., & Wickner, W. T. (2000) · The EMBO Journal · doi:10.1093/emboj/19.16.4393 · Cited by 71
Self-citation
Inactivation of the endoplasmic reticulum protein translocation factor, Sec61p, or its homolog, Ssh1p, does not affect peroxisome biogenesis
South, S. T., Baumgart‐Vogt, E., & Gould, S. J. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.221289498 · Cited by 59
Structural insight into the protein translocation channel
Clemons, W., Ménétret, J., Akey, C. W., & Rapoport, T. A. (2004) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2004.07.006 · Cited by 57
Prepro-carboxypeptidase Y and a truncated form of pre-invertase, but not full-length pre-invertase, can be posttranslationally translocated across microsomal vesicle membranes from Saccharomyces cerevisiae.
Hansen, W., & Walter, P. (1988) · The Journal of Cell Biology · doi:10.1083/jcb.106.4.1075 · Cited by 45
Translocation of a long amino‐terminal domain through ER membrane by following signal‐anchor sequence
Kida, Y., Mihara, K., & Sakaguchi, M. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600788 · Cited by 22
GENETICS AND BIOGENESIS OF CHLOROPLASTS AND
Neupert, W., Sebald, W., & Werner, S. (1976) · Cited by 18

Research works printed but not linked: 2

C. Milstein, G. G. Brownlee, T. M. Harrison, M. B. Mathews, Nature New Biol239, 117 (1972).
J. Luirink, I. Sinning, Biochim. Biophys. Acta1694, 17 (2004).

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Authors: Wickner, W., & Schekman, R.
Affiliations: Dartmouth College (US)
Corresponding author: Wickner, William
Schekman, Randy
ORCID: Wickner, William
Schekman, Randy
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 2005-12-02
Volume: 310
Issue: 5753
Pages: 1452-1456
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.1113752
OpenAlex: W2021288400
Cited by: 458
References: 96
Citations by year: 2026: 7 · 2025: 13 · 2024: 10 · 2023: 13 · 2022: 20 · 2021: 20 · 2020: 25 · 2019: 13 · 2018: 13 · 2017: 16 · 2016: 18 · 2015: 18 · 2014: 35 · 2013: 19 · 2012: 28
FWCI: 2.36
Type: journal article
Language: en
Open access: closed
Locations: Science (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
Keywords: protein translocation, biological membranes, organelle targeting, mitochondrial protein import, chloroplast protein import, substrate specificity, membrane lipid environment, energy coupling, subcellular compartmentalization
MeSH terms: Carrier Proteins, Endoplasmic Reticulum, Intracellular Membranes, Mitochondria, Protein Biosynthesis, Protein Folding, Peroxisomes, Protein Transport

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Protein Translocation Across Biological Membranes

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