The SND proteins constitute an alternative targeting route to the endoplasmic reticulum
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چکیده
منابع مشابه
Targeting pathways to the endoplasmic reticulum membrane.
The targeting of proteins to the endoplasmic reticulum (ER) membrane is the first step in the secretory pathway through which proteins are transported to the outside of the cell, the plasma membrane, and the luminal spaces and membranes of the endomembrane system. Proteins that undergo this targeting event carry a stretch of hydrophobic amino acids, usually at the amino terminus, that constitut...
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In the yeast Saccharomyces cerevisiae, only a subset of preproteins that are translocated across the ER membrane require the function of the signal recognition particle (SRP), suggesting that an alternative, SRP-independent pathway must exist (Hann, B.C., and P. Walter. 1991. Cell. 67:131-144). We have established that the two targeting pathways function in parallel. Mutant alleles of SEC62 and...
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Amino-terminal acetylation is probably the most common protein modification in eukaryotes with as many as 50%-80% of proteins reportedly altered in this way. Here we report a systematic analysis of the predicted N-terminal processing of cytosolic proteins versus those destined to be sorted to the secretory pathway. While cytosolic proteins were profoundly biased in favour of processing, we foun...
متن کاملTargeting expression of expanded polyglutamine proteins to the endoplasmic reticulum or mitochondria prevents their aggregation.
Aggregation of misfolded proteins is a characteristic of several neurodegenerative diseases. The huntingtin amino-terminal fragment with extended polyglutamine repeat forms aggregates closely associated with chaperones both in the cytoplasm and the nucleus. Because each cellular compartment contains distinct chaperones and because the molecular mechanisms controlling polyglutamine aggregation a...
متن کاملRoad to ruin: targeting proteins for degradation in the endoplasmic reticulum.
Some nascent proteins that fold within the endoplasmic reticulum (ER) never reach their native state. Misfolded proteins are removed from the folding machinery, dislocated from the ER into the cytosol, and degraded in a series of pathways collectively referred to as ER-associated degradation (ERAD). Distinct ERAD pathways centered on different E3 ubiquitin ligases survey the range of potential ...
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ژورنال
عنوان ژورنال: Nature
سال: 2016
ISSN: 0028-0836,1476-4687
DOI: 10.1038/nature20169