WIPI2b recruitment to phagophores and ATG16L1 binding are regulated by ULK1 phosphorylation.

Amphipathic Helix Autophagosome Autophagy Kinase WIPIs

Journal

EMBO reports
ISSN: 1469-3178
Titre abrégé: EMBO Rep
Pays: England
ID NLM: 100963049

Informations de publication

Date de publication:
16 Aug 2024
Historique:
received: 15 12 2023
accepted: 04 07 2024
revised: 21 06 2024
medline: 17 8 2024
pubmed: 17 8 2024
entrez: 16 8 2024
Statut: aheadofprint

Résumé

One of the key events in autophagy is the formation of a double-membrane phagophore, and many regulatory mechanisms underpinning this remain under investigation. WIPI2b is among the first proteins to be recruited to the phagophore and is essential for stimulating autophagy flux by recruiting the ATG12-ATG5-ATG16L1 complex, driving LC3 and GABARAP lipidation. Here, we set out to investigate how WIPI2b function is regulated by phosphorylation. We studied two phosphorylation sites on WIPI2b, S68 and S284. Phosphorylation at these sites plays distinct roles, regulating WIPI2b's association with ATG16L1 and the phagophore, respectively. We confirm WIPI2b is a novel ULK1 substrate, validated by the detection of endogenous phosphorylation at S284. Notably, S284 is situated within an 18-amino acid stretch, which, when in contact with liposomes, forms an amphipathic helix. Phosphorylation at S284 disrupts the formation of the amphipathic helix, hindering the association of WIPI2b with membranes and autophagosome formation. Understanding these intricacies in the regulatory mechanisms governing WIPI2b's association with its interacting partners and membranes, holds the potential to shed light on these complex processes, integral to phagophore biogenesis.

Identifiants

pubmed: 39152217
doi: 10.1038/s44319-024-00215-5
pii: 10.1038/s44319-024-00215-5
doi:

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : Wellcome Trust
ID : CC2134
Pays : United Kingdom
Organisme : Cancer Research UK (CRUK)
ID : CC1068
Organisme : Wellcome Trust
ID : CC2134
Pays : United Kingdom
Organisme : UKRI | Medical Research Council (MRC)
ID : CC1068
Organisme : Wellcome Trust
ID : CC2134
Pays : United Kingdom
Organisme : Wellcome Trust (WT)
ID : CC1068

Informations de copyright

© 2024. The Author(s).

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Auteurs

Andrea Gubas (A)

Molecular Cell Biology of Autophagy, The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.
Muscular Dystrophy UK, London, SE1 8QD, UK.

Eleanor Attridge (E)

Molecular Cell Biology of Autophagy, The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.

Harold Bj Jefferies (HB)

Molecular Cell Biology of Autophagy, The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.

Taki Nishimura (T)

Department of Biochemistry and Molecular Biology, Graduate School and Faculty of Medicine, The University of Tokyo, Tokyo, Japan.
PRESTO, Japan Science and Technology Agency, Chiyoda-ku, Tokyo, Japan.

Minoo Razi (M)

Molecular Cell Biology of Autophagy, The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.

Simone Kunzelmann (S)

Structural Biology Science Technology Platform, The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.

Yuval Gilad (Y)

The Weizmann Institute of Science, Rehovot, Israel.

Thomas J Mercer (TJ)

Genetech, 1 DNA Way, South San Francisco, CA, 94080, USA.

Michael M Wilson (MM)

The Babraham Institute, Cambridge, CB22 3AT, UK.

Adi Kimchi (A)

The Weizmann Institute of Science, Rehovot, Israel.

Sharon A Tooze (SA)

Molecular Cell Biology of Autophagy, The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK. Sharon.tooze@crick.ac.uk.

Classifications MeSH