Different effects of Sec61a, Sec62 and Sec63 depletion on transport of polypeptides into the endoplasmic reticulum of mammalian cells
نویسندگان
چکیده
Sven Lang, Julia Benedix, Sorin V. Fedeles, Stefan Schorr, Claudia Schirra, Nico Schäuble, Carolin Jalal, Markus Greiner, Sarah Haßdenteufel, Jörg Tatzelt, Birgit Kreutzer, Ludwig Edelmann, Elmar Krause, Jens Rettig, Stefan Somlo, Richard Zimmermann* and Johanna Dudek Medical Biochemistry and Molecular Biology, Saarland University D-66421, Homburg, Germany Internal Medicine, Yale School of Medicine, New Haven, CT 06520-8029, USA Institute of Physiology, Saarland University, D-66421, Homburg, Germany Neurobiochemistry, Adolf-Butenandt-Institute, Ludwig-Maximilians-University and German Center for Neurodegenerative Diseases, D-80336 Munich, Germany Clinic of Urology and Pediatric Urology, Saarland University Hospital, D-66421 Homburg, Germany Institute of Anatomy and Cell Biology, Saarland University, D-66421 Homburg, Germany
منابع مشابه
Different effects of Sec61α, Sec62 and Sec63 depletion on transport of polypeptides into the endoplasmic reticulum of mammalian cells.
Co-translational transport of polypeptides into the endoplasmic reticulum (ER) involves the Sec61 channel and additional components such as the ER lumenal Hsp70 BiP and its membrane-resident co-chaperone Sec63p in yeast. We investigated whether silencing the SEC61A1 gene in human cells affects co- and post-translational transport of presecretory proteins into the ER and post-translational membr...
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The metazoan Sec61 translocon transports polypeptides into and across the membrane of the endoplasmic reticulum via two major routes, a well-established co-translational pathway and a post-translational alternative. We have used two model substrates to explore the elements of a secretory protein precursor that preferentially direct it towards a co- or post-translational pathway for ER transloca...
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Because of similarity to their yeast orthologues, the two membrane proteins of the human endoplasmic reticulum (ER) Sec62 and Sec63 are expected to play a role in protein biogenesis in the ER. We characterized interactions between these two proteins as well as the putative interaction of Sec62 with ribosomes. These data provide further evidence for evolutionary conservation of Sec62/Sec63 inter...
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Genes that function in translocation of secretory protein precursors into the ER have been identified by a genetic selection for mutant yeast cells that fail to translocate a signal peptide-cytosolic enzyme hybrid protein. The new mutants, sec62 and sec63, are thermosensitive for growth and accumulate a variety of soluble secretory and vacuolar precursors whose electrophoretic mobilities coinci...
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The Sec61 translocon of the endoplasmic reticulum (ER) membrane forms an aqueous pore, allowing polypeptides to be transferred across or integrated into membranes. Protein translocation into the ER can occur co- and posttranslationally. In yeast, posttranslational translocation involves the heptameric translocase complex including its Sec62p and Sec63p subunits. The mammalian ER membrane contai...
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