Literature DB >> 11306271

Ribosome exchange revisited: a mechanism for translation-coupled ribosome detachment from the ER membrane.

M D Potter1, R M Seiser, C V Nicchitta.   

Abstract

In current models, ribosome release from the endoplasmic reticulum (ER) is coupled to the termination of protein translation. Thus, coincident with termination, membrane-bound ribosomes dissociate into their component subunits and are released into the cytosol. Here, we review past and current data and propose that the affinity of the ribosome for the ER membrane is decreased during translation, with ribosome release occurring when a membrane-bound ribosome is engaged in the synthesis of a protein lacking a signal sequence. Our model emphasizes a role for the conformation of the large ribosomal subunit in the regulation of membrane affinity and provides a mechanism for translation-coupled ribosome release.

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Year:  2001        PMID: 11306271     DOI: 10.1016/s0962-8924(00)01905-x

Source DB:  PubMed          Journal:  Trends Cell Biol        ISSN: 0962-8924            Impact factor:   20.808


  18 in total

Review 1.  Understanding the biogenesis of polytopic integral membrane proteins.

Authors:  R J Turner
Journal:  J Membr Biol       Date:  2003-04-01       Impact factor: 1.843

2.  Partitioning and translation of mRNAs encoding soluble proteins on membrane-bound ribosomes.

Authors:  Rachel S Lerner; Robert M Seiser; Tianli Zheng; Patrick J Lager; Mary C Reedy; Jack D Keene; Christopher V Nicchitta
Journal:  RNA       Date:  2003-09       Impact factor: 4.942

3.  Arf1p provides an unexpected link between COPI vesicles and mRNA in Saccharomyces cerevisiae.

Authors:  Mark Trautwein; Jörn Dengjel; Markus Schirle; Anne Spang
Journal:  Mol Biol Cell       Date:  2004-09-08       Impact factor: 4.138

4.  BiP modulates the affinity of its co-chaperone ERj1 for ribosomes.

Authors:  Julia Benedix; Patrick Lajoie; Himjyot Jaiswal; Carsten Burgard; Markus Greiner; Richard Zimmermann; Sabine Rospert; Erik L Snapp; Johanna Dudek
Journal:  J Biol Chem       Date:  2010-09-23       Impact factor: 5.157

5.  Stable ribosome binding to the endoplasmic reticulum enables compartment-specific regulation of mRNA translation.

Authors:  Samuel B Stephens; Rebecca D Dodd; Joseph W Brewer; Patrick J Lager; Jack D Keene; Christopher V Nicchitta
Journal:  Mol Biol Cell       Date:  2005-10-12       Impact factor: 4.138

6.  Ribosome binding to and dissociation from translocation sites of the endoplasmic reticulum membrane.

Authors:  Julia Schaletzky; Tom A Rapoport
Journal:  Mol Biol Cell       Date:  2006-07-05       Impact factor: 4.138

7.  mRNA translation is compartmentalized to the endoplasmic reticulum following physiological inhibition of cap-dependent translation.

Authors:  Rachel S Lerner; Christopher V Nicchitta
Journal:  RNA       Date:  2006-03-15       Impact factor: 4.942

8.  Different effects of Sec61α, Sec62 and Sec63 depletion on transport of polypeptides into the endoplasmic reticulum of mammalian cells.

Authors:  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; Johanna Dudek
Journal:  J Cell Sci       Date:  2012-02-28       Impact factor: 5.285

9.  Blocking variant surface glycoprotein synthesis in Trypanosoma brucei triggers a general arrest in translation initiation.

Authors:  Terry K Smith; Nadina Vasileva; Eva Gluenz; Stephen Terry; Neil Portman; Susanne Kramer; Mark Carrington; Shulamit Michaeli; Keith Gull; Gloria Rudenko
Journal:  PLoS One       Date:  2009-10-26       Impact factor: 3.240

10.  Evolutionary gain of function for the ER membrane protein Sec62 from yeast to humans.

Authors:  Linda Müller; Maria Diaz de Escauriaza; Patrick Lajoie; Melanie Theis; Martin Jung; Anika Müller; Carsten Burgard; Markus Greiner; Erik L Snapp; Johanna Dudek; Richard Zimmermann
Journal:  Mol Biol Cell       Date:  2010-01-13       Impact factor: 4.138

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