Document Detail


Determinants of the nucleocytoplasmic shuttling of muscle glycogen synthase.
MedLine Citation:
PMID:  15955076     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Muscle glycogen synthase (MGS) presents a nuclear speckled pattern in primary cultured human muscle and in 3T3-L1 cells deprived of glucose and with depleted glycogen reserves. Nuclear accumulation of the enzyme correlates inversely with cellular glycogen content. Although the glucose-induced export of MGS from the nucleus to the cytoplasm is blocked by leptomycin B, and therefore mediated by CRM1, no nuclear export signal was identified in the sequence of the protein. Deletion analysis shows that the region comprising amino acids 555-633 of human MGS, which encompasses an Arg-rich cluster involved in the allosteric activation of the enzyme by Glc6P, is crucial for its nuclear concentration and aggregation. Mutation of these Arg residues, which desensitizes the enzyme towards Glc6P, interferes with its nuclear accumulation. In contrast, the known phosphorylation sites of MGS that regulate its activity are not involved in the control of its subcellular distribution. Nuclear human MGS co-localizes with the promyelocytic leukaemia oncoprotein and p80-coilin, a marker of Cajal bodies. The subnuclear distribution of MGS is altered by incubation with transcription inhibitors. These observations suggest that, in addition to its metabolic function, MGS may participate in nuclear processes.
Authors:
Emili Cid; Daniel Cifuentes; Susanna Baqué; Juan C Ferrer; Joan J Guinovart
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The FEBS journal     Volume:  272     ISSN:  1742-464X     ISO Abbreviation:  FEBS J.     Publication Date:  2005 Jun 
Date Detail:
Created Date:  2005-06-15     Completed Date:  2005-08-10     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  101229646     Medline TA:  FEBS J     Country:  England    
Other Details:
Languages:  eng     Pagination:  3197-213     Citation Subset:  IM    
Affiliation:
Departament de Bioquímica i Biologia Molecular, Universitat de Barcelona, Spain.
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MeSH Terms
Descriptor/Qualifier:
3T3 Cells
Active Transport, Cell Nucleus / physiology*
Amino Acid Sequence
Animals
Arginine / genetics
Cell Nucleus Structures / metabolism
Cells, Cultured
Glycogen / metabolism
Glycogen Synthase / genetics,  metabolism*
Green Fluorescent Proteins / genetics,  metabolism
Humans
Karyopherins / metabolism
Mice
Molecular Sequence Data
Muscle, Skeletal / cytology,  metabolism*
Neoplasm Proteins / metabolism
Nuclear Localization Signals
Nuclear Proteins / metabolism
Phosphorylation
Receptors, Cytoplasmic and Nuclear / metabolism
Recombinant Proteins / genetics,  metabolism
Subcellular Fractions
Transcription Factors / metabolism
Tumor Suppressor Proteins
Chemical
Reg. No./Substance:
0/Karyopherins; 0/Neoplasm Proteins; 0/Nuclear Localization Signals; 0/Nuclear Proteins; 0/Pml protein, mouse; 0/Receptors, Cytoplasmic and Nuclear; 0/Recombinant Proteins; 0/Transcription Factors; 0/Tumor Suppressor Proteins; 0/exportin 1 protein; 136882-81-0/p80-coilin; 143220-95-5/PML protein, human; 147336-22-9/Green Fluorescent Proteins; 74-79-3/Arginine; 9005-79-2/Glycogen; EC 2.4.1.11/Glycogen Synthase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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