Document Detail

PIKfyve: a new fish in the growing pool of AMPK substrates.
MedLine Citation:
PMID:  24070423     Owner:  NLM     Status:  In-Data-Review    
Skeletal muscle is critical for whole-body glucose homoeostasis. Insulin and muscle contractions induced by exercise can increase glucose uptake through distinct intracellular signalling pathways involving PKB (protein kinase B)/Akt and AMPK (AMP-activated protein kinase) respectively. Whereas the proximal events governing these processes are becoming well understood, less is known about the regulation of the complex events necessary for the control of glucose uptake at the plasma membrane. In recent years, a number of common targets of AMPK and PKB/Akt have emerged as important components controlling glucose uptake, but the necessary phosphorylation events required for the control of glucose uptake have remained more elusive. In the current issue of the Biochemical Journal, Liu et al. identify that PIKfyve, a phosphoinositide phosphate kinase, is required for contraction-stimulated glucose uptake. They demonstrate that AMPK directly phosphorylates PIKfyve at Ser307, the same site as PKB/Akt, and that phosphorylation is increased in response to muscle contractions. These data provide compelling evidence for a new AMPK substrate that converges with PKB/Akt signalling and may be critical for the control of glucose uptake in skeletal muscle.
James S V Lally; Gregory R Steinberg
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  The Biochemical journal     Volume:  455     ISSN:  1470-8728     ISO Abbreviation:  Biochem. J.     Publication Date:  2013 Oct 
Date Detail:
Created Date:  2013-09-27     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  England    
Other Details:
Languages:  eng     Pagination:  e1-3     Citation Subset:  IM    
*Department of Medicine, McMaster University, 1200 Main St. W., Hamilton, Ontario, Canada, L8N 3Z5.
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