Autor: |
Liaci AM; Bijvoet Centre for Biomolecular Research, Structural Biochemistry Group, Utrecht University, Universiteitsweg 99, 3584 CG Utrecht, The Netherlands., Förster F; Bijvoet Centre for Biomolecular Research, Structural Biochemistry Group, Utrecht University, Universiteitsweg 99, 3584 CG Utrecht, The Netherlands. |
Jazyk: |
angličtina |
Zdroj: |
International journal of molecular sciences [Int J Mol Sci] 2021 Nov 01; Vol. 22 (21). Date of Electronic Publication: 2021 Nov 01. |
DOI: |
10.3390/ijms222111871 |
Abstrakt: |
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. |
Databáze: |
MEDLINE |
Externí odkaz: |
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