DOI: 10.1038/42276. Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation

Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation

10.1038/42276

Crossref journal-article

Springer Science and Business Media LLC

Nature (297)

Bibliography

Plemper, R. K., BÃ¶hmler, S., Bordallo, J., Sommer, T., & Wolf, D. H. (1997). Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature, 388(6645), 891â895.

Authors 5

Richard K. Plemper (first)
Sigrun Böhmler (additional)
Javier Bordallo (additional)
Thomas Sommer (additional)
Dieter H. Wolf (additional)

References 29 Referenced 455

Pryer, N. K., Wuestehube, L. J. & Schekman, R. Vesicle-mediated protein sorting. Annu. Rev. Biochem. 61, 471–516 (1992). / Annu. Rev. Biochem. by NK Pryer (1992)
Gething, M. J. & Sambrook, J. Protein folding in the cell. Nature 355, 33–45 (1992). (10.1038/355033a0) / Nature by MJ Gething (1992)
Kopito, R. R. ER quality control: the cytoplasmic connection. Cell 88, 427–430 (1997). / Cell by RR Kopito (1997)
Biederer, T., Volkwein, C. & Sommer, T. Degradation of subunits of the Sec61p complex, an integral component of the ER membrane, by the ubiquitin-proteasome pathway. EMBO J. 15, 2069–2076 (1996). / EMBO J. by T Biederer (1996)
Hiller, M. M., Finger, A., Schweiger, M. & Wolf, D. H. ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway. Science 273, 1725–1728 (1996). / Science by MM Hiller (1996)
Werner, E. D., Brodsky, J. L. & McCracken, A. A. Proteasome-dependent endoplasmic reticulum-associated protein degradation: an unconventional route to a familiar fate. Proc. Natl Acad. Sci. USA 93, 13797–13801 (1996). / Proc. Natl Acad. Sci. USA by ED Werner (1996)
Jensen, T. J.et al. Multiple proteolytic systems, including the proteasome, contribute to CFTR processing. Cell 83, 129–135 (1995). / Cell by TJ Jensen (1995)
Halaban, R.et al. Aberrant retention of tyrosinase in the endoplasmic reticulum mediates accelerated degradation of the enzyme and contributes to the dedifferentiated phenotype of amelanotic melanoma cells. Proc. Natl Acad. Sci. USA 94, 6210–6215 (1997). / Proc. Natl Acad. Sci. USA by R Halaban (1997)
Walter, P. & Johnson, A. E. Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane. Annu. Rev. Cell Biol. 10, 87–119 (1994). / Annu. Rev. Cell Biol. by P Walter (1994)
Rapoport, T. A., Jungnickel, B. & Kutay, U. Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes. Annu. Rev. Biochem. 65, 271–303 (1996). / Annu. Rev. Biochem. by TA Rapoport (1996)
Wiertz, E. J. H. J.et al. Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature 384, 432–438 (1996). (10.1038/384432a0) / Nature by EJHJ Wiertz (1996)
Lyman, S. K. & Schekman, R. Binding of secretory precursor polypeptides to a translocon subcomplex is regulated by BiP. Cell 88, 85–96 (1997). / Cell by SK Lyman (1997)
Finger, A., Knop, M. & Wolf, D. H. Analysis of two mutated vacuolar proteins reveals a degradation pathway in the endoplasmic reticulum or a related compartment of yeast. Eur. J. Biochem. 218, 565–574 (1993). / Eur. J. Biochem. by A Finger (1993)
Stirling, C. S., Rothblatt, J., Hosobuchi, M., Deshaies, R. & Schekman, R. Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum. Mol. Cell. Biol. 3, 129–142 (1992). / Mol. Cell. Biol. by CS Stirling (1992)
Panzner, S., Dreier, L., Hartmann, E., Kostka, S. & Rapoport, T. A. Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p. Cell 81, 561–570 (1995). / Cell by S Panzner (1995)
Finke, K.et al. Asecond trimeric complex containing homologs of the Sec61p complex functions in protein transport across the ER membrane of S. cerevisiae. EMBO J. 15, 1482–1494 (1996). / EMBO J. by K Finke (1996)
Feldheim, D., Rothblatt, J. & Schekman, R. Topology and functional domains of Sec63p, an endoplasmic reticulum membrane protein required for secretory protein translocation. Mol. Cell. Biol. 12, 3288–3296 (1992). / Mol. Cell. Biol. by D Feldheim (1992)
Corsi, A. K. & Schekman, R. The lumenal domain of Sec63p stimulates the ATPase activity of BiP and mediates BiP recruitment to the translocon in Saccharomyces cerevisiae. J. Cell Biol. 137, 1483–1493 (1997). / J. Cell Biol. by AK Corsi (1997)
Cyr, D. M., Langer, T. & Douglas, M. G. DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70. Trends Biochem. Sci. 19, 176–181 (1994). / Trends Biochem. Sci. by DM Cyr (1994)
Hanein, D.et al. Oligomeric rings of the Sec61p complex induced by ligands required for protein translocation. Cell 87, 721–732 (1996). / Cell by D Hanein (1996)
Scidmore, M. A., Okamura, H. H. & Rose, M. D. Genetic interactions between KAR2 and SEC63, encoding eukaryotic homologues of DnaK and DnaJ in the endoplasmic reticulum. Mol. Biol. Cell 4, 1145–1159 (1993). / Mol. Biol. Cell by MA Scidmore (1993)
Sanders, S. L., Whitfield, K. M., Vogel, J. P., Rose, M. D. & Schekman, R. Sec61p and BiP directly facilitate polypeptide translocation into the ER. Cell 69, 353–365 (1992). / Cell by SL Sanders (1992)
Esnault, Y., Blondel, M. -O., Deshaies, R. J., Schekman, R. & Képès, F. The yeast SSS1 gene is essential for secretory protein translocation and encodes a conserved protein of the endoplasmic reticulum. EMBO J. 12, 4083–4093 (1993). / EMBO J. by Y Esnault (1993)
Ng, D. T., Brown, J. D. & Walter, P. Signal sequences specify the targeting route to the endoplasmic reticulum membrane. J. Cell Biol. 134, 269–278 (1996). / J. Cell Biol. by DT Ng (1996)
Chen, P., Johnson, P., Sommer, T., Jentsch, S. & Hochstrasser, M. Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MAT α2 repressor. Cell 74, 357–369 (1993). / Cell by P Chen (1993)
Knop, M., Finger, A., Braun, T., Hellmuth, K. & Wolf, D. H. Der1, a novel protein specifically requires for endoplasmic reticulum degradation in yeast. EMBO J. 15, 753–763 (1996). / EMBO J. by M Knop (1996)
Hampton, R. Y., Gardner, R. G. & Rine, J. Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein. Mol. Biol. Cell 7, 2029–2044 (1994). / Mol. Biol. Cell by RY Hampton (1994)
Ausubel, F. M.et al. Current Protocols in Molecular Biology(Greene, New York, (1992)). / Current Protocols in Molecular Biology by FM Ausubel (1992)
Rose, M. D., Misra, L. M. & Vogel, J. P. Kar2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene. Cell 57, 1211–1221 (1989). / Cell by MD Rose (1989)

Dates

Type	When
Created	23 years ago (July 26, 2002, 4:37 a.m.)
Deposited	1 year, 5 months ago (Feb. 26, 2024, 1:08 p.m.)
Indexed	3 days, 5 hours ago (Aug. 20, 2025, 8:21 a.m.)
Issued	27 years, 11 months ago (Aug. 28, 1997)
Published	27 years, 11 months ago (Aug. 28, 1997)
Published Print	27 years, 11 months ago (Aug. 28, 1997)

Funders 0

None

BibTeX

@article{Plemper_1997, title={Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation}, volume={388}, ISSN={1476-4687}, url={http://dx.doi.org/10.1038/42276}, DOI={10.1038/42276}, number={6645}, journal={Nature}, publisher={Springer Science and Business Media LLC}, author={Plemper, Richard K. and Böhmler, Sigrun and Bordallo, Javier and Sommer, Thomas and Wolf, Dieter H.}, year={1997}, month=aug, pages={891–895} }

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