A portrait of the GET pathway as a surprisingly complicated young man

Many eukaryotic membrane proteins have a single C-terminal transmembrane domain that anchors them to a variety of organelles in secretory and endocytic pathways. These tail-anchored (TA) proteins are post-translationally inserted into the endoplasmic reticulum by molecular mechanisms that have long...

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Bibliographic Details
Published inTrends in biochemical sciences (Amsterdam. Regular ed.) Vol. 37; no. 10; pp. 411 - 417
Main Author Denic, Vladimir
Format Journal Article
LanguageEnglish
Published England Elsevier Ltd 01.10.2012
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Summary:Many eukaryotic membrane proteins have a single C-terminal transmembrane domain that anchors them to a variety of organelles in secretory and endocytic pathways. These tail-anchored (TA) proteins are post-translationally inserted into the endoplasmic reticulum by molecular mechanisms that have long remained mysterious. This review describes how, in just the past 5 years, intense research by a handful of laboratories has led to identification of all the key components of one such mechanism, the guided entry of TA proteins (GET) pathway, which is conserved from yeast to man. The GET pathway is both surprisingly complicated and yet more experimentally tractable than most other membrane insertion mechanisms, and is rapidly revealing new fundamental concepts in membrane protein biogenesis.
Bibliography:http://dx.doi.org/10.1016/j.tibs.2012.07.004
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ISSN:0968-0004
1362-4326
DOI:10.1016/j.tibs.2012.07.004