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First published online 11 April 2006
doi: 10.1242/jcs.02891

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Plectin scaffolds recruit energy-controlling AMP-activated protein kinase (AMPK) in differentiated myofibres

Martin Gregor^1,*, Aniko Zeöld^1,*, Susanne Oehler¹, Kerstin Andrä Marobela¹, Peter Fuchs¹, Günter Weigel², D. Graham Hardie³ and Gerhard Wiche^1,

¹ Department of Molecular Cell Biology, Max F. Perutz Laboratories, University of Vienna, A-1030 Vienna, Austria
² Department of Cardiothoracic Surgery, Medical University of Vienna, A-1090 Vienna, Austria
³ Division of Molecular Physiology, Wellcome Trust Biocentre, University of Dundee, Dundee, DD1 5EH, UK

Author for correspondence (e-mail: gerhard.wiche{at}univie.ac.at)

Accepted 17 January 2006

Plectin, a cytolinker protein greater than 500 kDa in size, has an important role as a mechanical stabiliser of cells. It interlinks the various cytoskeletal filament systems and anchors intermediate filaments to peripheral junctional complexes. In addition, there is increasing evidence that plectin acts as a scaffolding platform that controls the spatial and temporal localisation and interaction of signaling proteins. In this study we show that, in differentiated mouse myotubes, plectin binds to the regulatory 1 subunit of AMP-activated protein kinase (AMPK), the key regulatory enzyme of energy homeostasis. No interaction was observed in undifferentiated myoblasts, and plectin-deficient myotubes showed altered positioning of 1-AMPK. In addition we found that plectin affects the subunit composition of AMPK, because isoform 1 of the catalytic subunit decreased in proportion to isoform 2 during in vitro differentiation of plectin^-/- myotubes. In plectin-deficient myocytes we could also detect a higher level of activated (Thr172-phosphorylated) AMPK, compared with wild-type cells. Our data suggest a differentiation-dependent association of plectin with AMPK, where plectin selectively stabilises 1-1 AMPK complexes by binding to the 1 regulatory subunit. The distinct plectin expression patterns in different fibre types combined with its involvement in the regulation of isoform compositions of AMPK complexes could provide a mechanism whereby cytoarchitecture influences energy homeostasis.

Key words: Cytoskeleton, Cytolinker proteins, AMPK regulation, Myoblast differentiation, Z-lines

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