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 BIN/amphiphysin/Rvs (BAR) proteins shape lipid membranes into functional shapes and compartments in a broad range of cellular processes. However, how a protein generates distinct forms of membrane curvature and how these states are regulated is unknown. We find that endophilin A1 uses different structures and mechanisms to generate tubes or vesicles. Phosphorylation toggles a conformational switch between these two structures, potentially acting as a regulator of membrane curvature in vivo. These findings may also explain how other proteins, including the BAR protein family, generate different shapes and are regulated in a large number of membrane remodeling processes.

Endophilin A1 induces different membrane shapes using a conformational switch that is regulated by phosphorylation