Phosphatidylinositol 3-phosphate 5-kinase (PIKfyve) is an AMPK target participating in contraction-stimulated glucose uptake in skeletal muscle. - 2013
Glucose Transporter Type 4; Insulin; Phosphatidylinositol Phosphates; phosphatidylinositol 3,5-diphosphate; Aminoimidazole Carboxamide; imidazolecarboxamide; Phosphatidylinositol 3-Kinase; AMP-Activated Protein Kinases; Glucose; AMP-Activated Protein Kinases/genetics; AMP-Activated Protein Kinases/metabolism; Aminoimidazole Carboxamide/analogs & derivatives; Aminoimidazole Carboxamide/metabolism; Animals; Cell Line; Glucose/metabolism; Glucose Transporter Type 4/metabolism; Humans; Insulin/metabolism; Male; Muscle Contraction/physiology; Muscle, Skeletal/enzymology; Muscle, Skeletal/metabolism; Opossums; Phosphatidylinositol 3-Kinase/genetics; Phosphatidylinositol 3-Kinase/metabolism; Phosphatidylinositol Phosphates/metabolism; Phosphorylation; Rats; Rats, Wistar; AMP-activated protein kinase (AMPK); Contraction; Glucose uptake; Protein kinase B (PKB); PtdIns(3,5)P2; Biochemistry; Molecular Biology; Cell Biology
Abstract :
[en] PIKfyve (FYVE domain-containing phosphatidylinositol 3-phosphate 5-kinase), the lipid kinase that phosphorylates PtdIns3P to PtdIns(3,5)P2, has been implicated in insulin-stimulated glucose uptake. We investigated whether PIKfyve could also be involved in contraction/AMPK (AMP-activated protein kinase)-stimulated glucose uptake in skeletal muscle. Incubation of rat epitrochlearis muscles with YM201636, a selective PIKfyve inhibitor, reduced contraction- and AICAriboside (5-amino-4-imidazolecarboxamide riboside)-stimulated glucose uptake. Consistently, PIKfyve knockdown in C2C12 myotubes reduced AICAriboside-stimulated glucose transport. Furthermore, muscle contraction increased PtdIns(3,5)P2 levels and PIKfyve phosphorylation. AMPK phosphorylated PIKfyve at Ser307 both in vitro and in intact cells. Following subcellular fractionation, PIKfyve recovery in a crude intracellular membrane fraction was increased in contracting versus resting muscles. Also in opossum kidney cells, wild-type, but not S307A mutant, PIKfyve was recruited to endosomal vesicles in response to AMPK activation. We propose that PIKfyve activity is required for the stimulation of skeletal muscle glucose uptake by contraction/AMPK activation. PIKfyve is a new AMPK substrate whose phosphorylation at Ser307 could promote PIKfyve translocation to endosomes for PtdIns(3,5)P2 synthesis to facilitate GLUT4 (glucose transporter 4) translocation.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Liu, Yang; *Université catholique de Louvain, de Duve Institute, Avenue Hippocrate, 75, B-1200 Brussels, Belgium
Lai, Yu-Chiang; Universite Catholique de Louvain, De Duve Institute, B-1200 Brussels, Belgium
Hill, Elaine V; Department of Biochemistry, School of Medical Sciences, University of Bristol, Bristol BS8 1TD, United Kingdom
Tyteca, Donatienne; Universite Catholique de Louvain, De Duve Institute, B-1200 Brussels, Belgium
Carpentier, Sarah; Universite Catholique de Louvain, De Duve Institute, B-1200 Brussels, Belgium
Ingvaldsen, Ada; National Institute of Occupational Health, Oslo, Norway
Vertommen, Didier; Universite Catholique de Louvain, De Duve Institute, B-1200 Brussels, Belgium
Lantier, Louise; INSERM, U1016, Institut Cochin, 75014 Paris, France ; CNRS, UMR8104, Universite Paris Descartes, 75014 Paris, France
Foretz, Marc; INSERM, U1016, Institut Cochin, 75014 Paris, France ; CNRS, UMR8104, Universite Paris Descartes, 75014 Paris, France
Dequiedt, Franck ; Université de Liège - ULiège > Unités de recherche interfacultaires > GIGA-Research
Courtoy, Pierre J; Universite Catholique de Louvain, De Duve Institute, B-1200 Brussels, Belgium
Viollet, Benoît; INSERM, U1016, Institut Cochin, 75014 Paris, France ; CNRS, UMR8104, Universite Paris Descartes, 75014 Paris, France
Shepherd, Peter R; Maurice Wilkins Centre for Molecular Biodiscovery, Department of Molecular Medicine and Pathology, University of Auckland, Auckland 1042, New Zealand
Tavaré, Jeremy M; Department of Biochemistry, School of Medical Sciences, University of Bristol, Bristol BS8 1TD, United Kingdom
Jensen, Jørgen; National Institute of Occupational Health, Oslo, Norway
Rider, Mark H; Universite Catholique de Louvain, De Duve Institute, B-1200 Brussels, Belgium
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