WHAMM initiates autolysosome tubulation by promoting actin polymerization on autolysosomes.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 31420534.
- Also identified by DOI 10.1038/s41467-019-11694-9 and PMC identifier 6697732.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
WHAMM, a member of the Wiskott-Aldrich syndrome protein (WASP) family, is an actin nucleation promoting factor (NPF) that also associates with membranes and microtubules. Here we report that WHAMM is required for autophagic lysosome reformation (ALR). WHAMM knockout causes impairment of autolysosome tubulation, which results in accumulation of enlarged autolysosomes during prolonged starvation. Mechanistically, WHAMM is recruited to the autolysosome membrane through its specific interaction with PI(4,5)P<sub>2</sub>. WHAMM then works as an NPF which promotes assembly of an actin scaffold on the surface of the autolysosome to promote autolysosome tubulation. Our study demonstrates an unexpected role of the actin scaffold in regulating autophagic lysosome reformation.
Medical subject headings
- Actins
- Autophagy
- Lysosomes
- Membrane Proteins
- Microtubule-Associated Proteins