Myristoylation confers noncanonical AMPK functions in autophagy selectivity and mitochondrial surveillance View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2015-12

AUTHORS

Jiyong Liang, Zhi-Xiang Xu, Zhiyong Ding, Yiling Lu, Qinghua Yu, Kaitlin D. Werle, Ge Zhou, Yun-Yong Park, Guang Peng, Michael J. Gambello, Gordon B. Mills

ABSTRACT

AMP-activated protein kinase (AMPK) plays a central role in cellular energy sensing and bioenergetics. However, the role of AMPK in surveillance of mitochondrial damage and induction of mitophagy remains unclear. We demonstrate herein that AMPK is required for efficient mitophagy. Mitochondrial damage induces a physical association of AMPK with ATG16-ATG5-12 and an AMPK-dependent recruitment of the VPS34 and ATG16 complexes with the mitochondria. Targeting AMPK to the mitochondria is both sufficient to induce mitophagy and to promote cell survival. Recruitment of AMPK to the mitochondria requires N-myristoylation of AMPKβ by the type-I N-myristoyltransferase 1 (NMT1). Our data support a spatiotemporal model wherein recruitment of AMPK in association with components of the VPS34 and ATG16 complex to damaged mitochondria regulates selective mitophagy to maintain cancer cell viability. More... »

PAGES

7926

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/ncomms8926

DOI

http://dx.doi.org/10.1038/ncomms8926

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1002624637

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/26272043


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