tailieunhanh - Báo cáo khoa học: Determinants of the nucleocytoplasmic shuttling of muscle glycogen synthase

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. | ềFEBS Journal Determinants of the nucleocytoplasmic shuttling of muscle glycogen synthase Emili Cid1 Daniel Cifuentes1 2 Susanna Baque1 Juan C. Ferrer1 and Joan J. Guinovart1 2 1 Departament de Bioquimica i Biologia Molecular Universitat de Barcelona Spain 2 Institut de Recerca Biomedica de Barcelona-Parc Cientific de Barcelona Universitat de Barcelona Spain Keywords glycogen green fluorescent protein muscle glycogen synthase nucleocytoplasmic translocation glucose 6-phosphate Correspondence J. J. Guinovart Institut de Recerca Biomedica de Barcelona-Parc Cientific de Barcelona c Josep Samitier 4-5 E-08028 Barcelona Spain Fax 34 934037114 Tel 34 934037163 E-mail guinovart@ Present address The Rockefeller University New York NY USA Received 18 November 2004 revised 24 March 2005 accepted 25 April2005 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 colocalizes 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. .

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