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  The Sec61 complex is essential for the insertion of proteins into the membrane of the endoplasmic reticulum.

Oliver, J., Jungnickel, B., Görlich, D., Rapoport, T. A., & High, S. (1995). The Sec61 complex is essential for the insertion of proteins into the membrane of the endoplasmic reticulum. FEBS Letters, 362(2), 126-130.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0015-3BF5-0 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-C500-D
Genre: Journal Article

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Oliver, J., Author
Jungnickel, B., Author
Görlich, D.1, Author              
Rapoport, T. A., Author
High, S., Author
Affiliations:
1Department of Cellular Logistics, MPI for biophysical chemistry, Max Planck Society, ou_578574              

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 Abstract: Cross-linking studies have implicated Sec61α as the principal component adjacent to newly synthesised membrane proteins during insertion into the endoplasmic reticulum. Using proteoliposomes which have been reconstituted from purified components of the endoplasmic reticulum [Görlich, D and Rapoport, T.A., Cell 75 (1993) 615–630] we have found that the Sec61 complex, consisting of three subunits, is essential for the insertion of single-spanning membrane proteins. This is true for signal-anchor proteins of both orientations, and for proteins with a cleavable signal sequence. These results support the view that Sec61α is a major component of the ER translocation site and promotes both the insertion of membrane proteins and the translocation of secretory proteins.

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Language(s): eng - English
 Dates: 1995-04-03
 Publication Status: Published in print
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Title: FEBS Letters
Source Genre: Journal
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Pages: - Volume / Issue: 362 (2) Sequence Number: - Start / End Page: 126 - 130 Identifier: -