Positive zip coding in small protein translocation

Most newly synthesized proteins destined for the secretory pathway contain a signal peptide (SP) that triggers cotranslational translocation into the endoplasmic reticulum (ER). However, how small polypeptides undergo ER translocation is not fully understood. In this issue of JBC, Guo et al. describ...

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Bibliographic Details
Published in:The Journal of biological chemistry 2018-02, Vol.293 (6), p.1908-1909
Main Authors: Okamoto, Yukari, Shikano, Sojin
Format: Article
Language:English
Subjects:
charge
Editors' Picks Highlights
endoplasmic reticulum (ER)
Endoplasmic Reticulum - genetics
Endoplasmic Reticulum - metabolism
Peptides - chemistry
Peptides - genetics
Peptides - metabolism
positive
posttranslational
Proinsulin - chemistry
Proinsulin - genetics
Proinsulin - metabolism
Protein Biosynthesis
Protein Sorting Signals
Protein Transport
ribosome
secretion
signal peptide
signal recognition particle (SRP)
Signal Recognition Particle - genetics
Signal Recognition Particle - metabolism
translocation
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Description
Summary:Most newly synthesized proteins destined for the secretory pathway contain a signal peptide (SP) that triggers cotranslational translocation into the endoplasmic reticulum (ER). However, how small polypeptides undergo ER translocation is not fully understood. In this issue of JBC, Guo et al. describe a mechanism for posttranslational translocation of small secretory proteins featuring a positive charge within the SP N-terminal region. Defects in this element disrupt proper secretion and explain the effects of genetic mutations associated with one type of diabetes.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.H118.001415