期刊
NATURE REVIEWS MOLECULAR CELL BIOLOGY
卷 11, 期 12, 页码 885-890出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nrm3008
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- Deutsche Forschungsgemeinschaft, Germany [SFB642]
Despite their distinct biological functions, there is a surprising similarity between the composition of the machinery that imports proteins into peroxisomes and the machinery that degrades endoplasmic reticulum (ER)-associated proteins. The basis of this similarity lies in the fact that both machineries make use of the same basic mechanistic principle: the tagging of a substrate by monoubiquitylation or polyubiquitylation and its subsequent recognition and ATP-dependent removal from a membrane by ATPases of the ATPases associated with diverse cellular activities (AAA) family of proteins. We propose that the ER-associated protein degradation (ERAD)-like removal of the peroxisomal import receptor is mechanically coupled to protein translocation into the organelle, giving rise to a new concept of export-driven import.
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