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Phosphorylation regulates the binding of autophagy receptors to FIP200 Claw domain for selective aut...

Phosphorylation regulates the binding of autophagy receptors to FIP200 Claw domain for selective aut...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_7866f28ceca14b898aab485fec664bfc

Phosphorylation regulates the binding of autophagy receptors to FIP200 Claw domain for selective autophagy initiation

About this item

Full title

Phosphorylation regulates the binding of autophagy receptors to FIP200 Claw domain for selective autophagy initiation

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2021-03, Vol.12 (1), p.1570-1570, Article 1570

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

The ULK complex initiates the autophagosome formation, and has recently been implicated in selective autophagy by interacting with autophagy receptors through its FIP200 subunit. However, the structural mechanism underlying the interactions of autophagy receptors with FIP200 and the relevant regulatory mechanism remain elusive. Here, we discover th...

Alternative Titles

Full title

Phosphorylation regulates the binding of autophagy receptors to FIP200 Claw domain for selective autophagy initiation

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_7866f28ceca14b898aab485fec664bfc

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_7866f28ceca14b898aab485fec664bfc

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-021-21874-1

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