The ribosome-Sec61 translocon complex forms a cytosolically restricted environment for early polytopic membrane protein folding

Melissa A. Patterson, Anannya Bandyopadhyay, Prasanna K. Devaraneni, Josha Woodward, Leeann Rooney, Zhongying Yang, William Skach

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Background: Mechanisms that guide membrane protein folding in the endoplasmic reticulum membrane remain unresolved. Results: During aquaporin-4 synthesis, extracellular peptides loops enter the endoplasmic reticulum lumen sequentially, whereas delivery of cytosolic loops is actively delayed. Conclusion: The assembled ribosome translocon complex (RTC) shields large regions of the protein from the cytosol throughout synthesis. Significance: Early membrane protein folding occurs in a proteinaceous environment provided by the RTC.

Original languageEnglish (US)
Pages (from-to)28944-28952
Number of pages9
JournalJournal of Biological Chemistry
Volume290
Issue number48
DOIs
StatePublished - Nov 27 2015

Fingerprint

Protein folding
Protein Folding
Ribosomes
Endoplasmic Reticulum
Membrane Proteins
Aquaporin 4
Cytosol
Membranes
Peptides
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

Patterson, M. A., Bandyopadhyay, A., Devaraneni, P. K., Woodward, J., Rooney, L., Yang, Z., & Skach, W. (2015). The ribosome-Sec61 translocon complex forms a cytosolically restricted environment for early polytopic membrane protein folding. Journal of Biological Chemistry, 290(48), 28944-28952. https://doi.org/10.1074/jbc.M115.672261

The ribosome-Sec61 translocon complex forms a cytosolically restricted environment for early polytopic membrane protein folding. / Patterson, Melissa A.; Bandyopadhyay, Anannya; Devaraneni, Prasanna K.; Woodward, Josha; Rooney, Leeann; Yang, Zhongying; Skach, William.

In: Journal of Biological Chemistry, Vol. 290, No. 48, 27.11.2015, p. 28944-28952.

Research output: Contribution to journalArticle

Patterson, MA, Bandyopadhyay, A, Devaraneni, PK, Woodward, J, Rooney, L, Yang, Z & Skach, W 2015, 'The ribosome-Sec61 translocon complex forms a cytosolically restricted environment for early polytopic membrane protein folding', Journal of Biological Chemistry, vol. 290, no. 48, pp. 28944-28952. https://doi.org/10.1074/jbc.M115.672261
Patterson, Melissa A. ; Bandyopadhyay, Anannya ; Devaraneni, Prasanna K. ; Woodward, Josha ; Rooney, Leeann ; Yang, Zhongying ; Skach, William. / The ribosome-Sec61 translocon complex forms a cytosolically restricted environment for early polytopic membrane protein folding. In: Journal of Biological Chemistry. 2015 ; Vol. 290, No. 48. pp. 28944-28952.
@article{ec154dc2691b4963b832477452f06a95,
title = "The ribosome-Sec61 translocon complex forms a cytosolically restricted environment for early polytopic membrane protein folding",
abstract = "Background: Mechanisms that guide membrane protein folding in the endoplasmic reticulum membrane remain unresolved. Results: During aquaporin-4 synthesis, extracellular peptides loops enter the endoplasmic reticulum lumen sequentially, whereas delivery of cytosolic loops is actively delayed. Conclusion: The assembled ribosome translocon complex (RTC) shields large regions of the protein from the cytosol throughout synthesis. Significance: Early membrane protein folding occurs in a proteinaceous environment provided by the RTC.",
author = "Patterson, {Melissa A.} and Anannya Bandyopadhyay and Devaraneni, {Prasanna K.} and Josha Woodward and Leeann Rooney and Zhongying Yang and William Skach",
year = "2015",
month = "11",
day = "27",
doi = "10.1074/jbc.M115.672261",
language = "English (US)",
volume = "290",
pages = "28944--28952",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "48",

}

TY - JOUR

T1 - The ribosome-Sec61 translocon complex forms a cytosolically restricted environment for early polytopic membrane protein folding

AU - Patterson, Melissa A.

AU - Bandyopadhyay, Anannya

AU - Devaraneni, Prasanna K.

AU - Woodward, Josha

AU - Rooney, Leeann

AU - Yang, Zhongying

AU - Skach, William

PY - 2015/11/27

Y1 - 2015/11/27

N2 - Background: Mechanisms that guide membrane protein folding in the endoplasmic reticulum membrane remain unresolved. Results: During aquaporin-4 synthesis, extracellular peptides loops enter the endoplasmic reticulum lumen sequentially, whereas delivery of cytosolic loops is actively delayed. Conclusion: The assembled ribosome translocon complex (RTC) shields large regions of the protein from the cytosol throughout synthesis. Significance: Early membrane protein folding occurs in a proteinaceous environment provided by the RTC.

AB - Background: Mechanisms that guide membrane protein folding in the endoplasmic reticulum membrane remain unresolved. Results: During aquaporin-4 synthesis, extracellular peptides loops enter the endoplasmic reticulum lumen sequentially, whereas delivery of cytosolic loops is actively delayed. Conclusion: The assembled ribosome translocon complex (RTC) shields large regions of the protein from the cytosol throughout synthesis. Significance: Early membrane protein folding occurs in a proteinaceous environment provided by the RTC.

UR - http://www.scopus.com/inward/record.url?scp=84948452827&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84948452827&partnerID=8YFLogxK

U2 - 10.1074/jbc.M115.672261

DO - 10.1074/jbc.M115.672261

M3 - Article

C2 - 26254469

AN - SCOPUS:84948452827

VL - 290

SP - 28944

EP - 28952

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 48

ER -