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 Human ALIX is involved in many essential cellular processes. The carboxy (C)-terminal proline-rich domain (PRD) of ALIX, which interacts with multiple partners, has eluded analysis owing to the presence of polyproline stretches that hinder recombinant protein production. By dividing it into two fragments, the amino (N)- and the C-terminal portions, we carry out a detailed biophysical investigation of ALIX-PRD. The disordered N-terminal fragment comprises three proline-rich motifs that compete for binding to its partner, TSG101-UEV. In contrast, the C-terminal fragment forms reversible amyloids modulated by tyrosine phosphorylation, the first known example where posttranslational modifications dictate the dissolution of amyloid fibrils. This study illustrates the mechanistic interdependence of multivalency brought out by polymerization of ALIX-PRD and its effect on ALIX function.

Proline-rich domain of human ALIX contains multiple TSG101-UEV interaction sites and forms phosphorylation-mediated reversible amyloids