Journal
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume 22, Issue 21, Pages -Publisher
MDPI
DOI: 10.3390/ijms222111871
Keywords
signal peptide; signal peptidase; ER translocon; endoplasmic reticulum; protein targeting; chaperones; protein translocation
Funding
- ERC Consolidator Grant [724425]
- European Research Council (ERC) [724425] Funding Source: European Research Council (ERC)
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Cleavable and non-cleavable signal sequences target a quarter of the human proteome to the ER. Interaction between these signal sequences and ER targeting machinery determines protein location and translocation fidelity, as discussed in recent insights from structural biology.
Cleavable endoplasmic reticulum (ER) signal peptides (SPs) and other non-cleavable signal sequences target roughly a quarter of the human proteome to the ER. These short peptides, mostly located at the N-termini of proteins, are highly diverse. For most proteins targeted to the ER, it is the interactions between the signal sequences and the various ER targeting and translocation machineries such as the signal recognition particle (SRP), the protein-conducting channel Sec61, and the signal peptidase complex (SPC) that determine the proteins' target location and provide translocation fidelity. In this review, we follow the signal peptide into the ER and discuss the recent insights that structural biology has provided on the governing principles of those interactions.
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