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Updated: May 11, 2026

Oligopeptide Competition Assay for Phosphorylation Site Determination
Published on: May 18, 2017
AMPK connects energy stress to PIK3C3/VPS34 regulation
1Department of Oral Biochemistry and Molecular Biology; Research Center for Tooth and Periodontal Tissue Regeneration; School of Dentistry; Kyung Hee University; Seoul, Korea.
Abstract:
The class III phosphatidylinositol (PtdIns)-3 kinase, PIK3C3/VPS34, forms multiple complexes and regulates a variety of cellular functions, especially in intracellular vesicle trafficking and autophagy. Even though PtdIns3P, the product of PIK3C3, is thought to be a critical membrane marker for the autophagosome, it is unclear how PIK3C3 is regulated in response to autophagy-inducing stimuli. A complexity of PIK3C3 biology is due in part to the existence of multiple complexes, of which the ATG14- or UVRAG-containing complexes play important roles in autophagy. We recently discovered differential regulation of distinct PIK3C3 complexes in response to energy starvation and showed a mechanism by which AMPK directly phosphorylates PIK3C3 and BECN1 to regulate non- and pro-autophagic PIK3C3 complexes, respectively.
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