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JCS ePress
online publication date 11 Apr 2006
doi: 10.1242/jcs.02891
Research Article
Plectin scaffolds recruit energy-controlling AMP-activated protein kinase (AMPK) in differentiated myofibres
Martin Gregor,
Aniko Zeöld,
Susanne Oehler,
Kerstin Andrä Marobela,
Peter Fuchs,
Günter Weigel,
D. Graham Hardie,
and
Gerhard Wiche*
* Author for correspondence (e-mail: gerhard.wiche{at}univie.ac.at)
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.
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© The Company of Biologists Ltd 2006
