Snf1/AMP-activated protein kinase activates Arf3p to promote invasive yeast growth via a non-canonical GEF domain

Jia-Wei Hsu, Kuan-Jung Chen and Fang-Jen S. Lee ()
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Jia-Wei Hsu: Institute of Molecular Medicine, College of Medicine, National Taiwan University
Kuan-Jung Chen: Institute of Molecular Medicine, College of Medicine, National Taiwan University
Fang-Jen S. Lee: Institute of Molecular Medicine, College of Medicine, National Taiwan University

Nature Communications, 2015, vol. 6, issue 1, 1-8

Abstract: Abstract Active GTP-bound Arf GTPases promote eukaryotic cell membrane trafficking and cytoskeletal remodelling. Arf activation is accelerated by guanine nucleotide-exchange factors (GEFs) using the critical catalytic glutamate in all known Sec7 domain sequences. Yeast Arf3p, a homologue of mammalian Arf6, is required for yeast invasive responses to glucose depletion. Here we identify Snf1p as a GEF that activates Arf3p when energy is limited. SNF1 is the yeast homologue of AMP-activated protein kinase (AMPK), which is a key regulator of cellular energy homeostasis. As activation of Arf3p does not depend on the Snf1p kinase domain, assay of regulatory domain fragments yield evidence that the C-terminal hydrophobic α-helix core of Snf1p is a non-canonical GEF for Arf3p activation. Thus, our study reveals a novel mechanism for regulating cellular responses to energy deprivation, in particular invasive cell growth, through direct Arf activation by Snf1/AMPK.

Date: 2015
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DOI: 10.1038/ncomms8840

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