Myristoylation confers noncanonical AMPK functions in autophagy selectivity and mitochondrial surveillance

Jiyong Liang (), Zhi-Xiang Xu, Zhiyong Ding, Yiling Lu, Qinghua Yu, Kaitlin D. Werle, Ge Zhou, Yun-Yong Park, Guang Peng, Michael J. Gambello and Gordon B. Mills ()
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Jiyong Liang: The University of Texas MD Anderson Cancer Center
Zhi-Xiang Xu: Comprehensive Cancer Center, University of Alabama at Birmingham
Zhiyong Ding: The University of Texas MD Anderson Cancer Center
Yiling Lu: The University of Texas MD Anderson Cancer Center
Qinghua Yu: The University of Texas MD Anderson Cancer Center
Kaitlin D. Werle: Comprehensive Cancer Center, University of Alabama at Birmingham
Ge Zhou: The University of Texas MD Anderson Cancer Center
Yun-Yong Park: The University of Texas MD Anderson Cancer Center
Guang Peng: The University of Texas MD Anderson Cancer Center
Michael J. Gambello: University of Texas Health Science Center at Houston
Gordon B. Mills: The University of Texas MD Anderson Cancer Center

Nature Communications, 2015, vol. 6, issue 1, 1-14

Abstract: 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.

Date: 2015
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DOI: 10.1038/ncomms8926

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