English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Significance Lacking a canonical signal peptide for translocation into the endoplasmic reticulum, galectin-3 (Gal3) is exported by unconventional secretion to play key roles in various cellular processes of fundamental importance. However, molecular details about the sorting components, the signals involved, and the underlying mechanism have remained elusive. Here, we identify a highly conserved tetrapeptide motif P(S/T)AP in the amino-terminal domain of Gal3 that directly interacts with the endosomal sorting complex required for transport (ESCRT) component Tsg101, resulting in exosomal release. This study thus defines a unique molecular mechanism based on a late domain-like motif known from many viruses by which an endogenous non-ESCRT protein is secreted in exosomes.

Molecular mechanism to recruit galectin-3 into multivesicular bodies for polarized exosomal secretion