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

Martin Gregor, A. Zeöld, Susanne Oehler, Kerstin Andrä Marobela, Peter Fuchs, Günter Weigel, D. Graham Hardie, Gerhard Wiche

Research output: Contribution to journalArticle

48 Citations (Scopus)

Abstract

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 γ1 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 γ1-AMPK. In addition we found that plectin affects the subunit composition of AMPK, because isoform α1 of the catalytic subunit decreased in proportion to isoform α2 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 α1-γ1 AMPK complexes by binding to the γ1 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.

Original languageEnglish
Pages (from-to)1864-1875
Number of pages12
JournalJournal of Cell Science
Volume119
Issue number9
DOIs
Publication statusPublished - May 1 2006

Fingerprint

Plectin
AMP-Activated Protein Kinases
Skeletal Muscle Fibers
Protein Isoforms
Plakins
Homeostasis
Intermediate Filaments
Myoblasts
Cytoskeleton
Muscle Cells
Catalytic Domain

Keywords

  • AMPK regulation
  • Cytolinker proteins
  • Cytoskeleton
  • Myoblast differentiation
  • Z-lines

ASJC Scopus subject areas

  • Cell Biology

Cite this

Plectin scaffolds recruit energy-controlling AMP-activated protein kinase (AMPK) in differentiated myofibres. / Gregor, Martin; Zeöld, A.; Oehler, Susanne; Marobela, Kerstin Andrä; Fuchs, Peter; Weigel, Günter; Hardie, D. Graham; Wiche, Gerhard.

In: Journal of Cell Science, Vol. 119, No. 9, 01.05.2006, p. 1864-1875.

Research output: Contribution to journalArticle

Gregor, M, Zeöld, A, Oehler, S, Marobela, KA, Fuchs, P, Weigel, G, Hardie, DG & Wiche, G 2006, 'Plectin scaffolds recruit energy-controlling AMP-activated protein kinase (AMPK) in differentiated myofibres', Journal of Cell Science, vol. 119, no. 9, pp. 1864-1875. https://doi.org/10.1242/jcs.02891
Gregor, Martin ; Zeöld, A. ; Oehler, Susanne ; Marobela, Kerstin Andrä ; Fuchs, Peter ; Weigel, Günter ; Hardie, D. Graham ; Wiche, Gerhard. / Plectin scaffolds recruit energy-controlling AMP-activated protein kinase (AMPK) in differentiated myofibres. In: Journal of Cell Science. 2006 ; Vol. 119, No. 9. pp. 1864-1875.
@article{c7ecf85912994100b08ca22bae7864c1,
title = "Plectin scaffolds recruit energy-controlling AMP-activated protein kinase (AMPK) in differentiated myofibres",
abstract = "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 γ1 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 γ1-AMPK. In addition we found that plectin affects the subunit composition of AMPK, because isoform α1 of the catalytic subunit decreased in proportion to isoform α2 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 α1-γ1 AMPK complexes by binding to the γ1 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.",
keywords = "AMPK regulation, Cytolinker proteins, Cytoskeleton, Myoblast differentiation, Z-lines",
author = "Martin Gregor and A. Ze{\"o}ld and Susanne Oehler and Marobela, {Kerstin Andr{\"a}} and Peter Fuchs and G{\"u}nter Weigel and Hardie, {D. Graham} and Gerhard Wiche",
year = "2006",
month = "5",
day = "1",
doi = "10.1242/jcs.02891",
language = "English",
volume = "119",
pages = "1864--1875",
journal = "Journal of Cell Science",
issn = "0021-9533",
publisher = "Company of Biologists Ltd",
number = "9",

}

TY - JOUR

T1 - Plectin scaffolds recruit energy-controlling AMP-activated protein kinase (AMPK) in differentiated myofibres

AU - Gregor, Martin

AU - Zeöld, A.

AU - Oehler, Susanne

AU - Marobela, Kerstin Andrä

AU - Fuchs, Peter

AU - Weigel, Günter

AU - Hardie, D. Graham

AU - Wiche, Gerhard

PY - 2006/5/1

Y1 - 2006/5/1

N2 - 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 γ1 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 γ1-AMPK. In addition we found that plectin affects the subunit composition of AMPK, because isoform α1 of the catalytic subunit decreased in proportion to isoform α2 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 α1-γ1 AMPK complexes by binding to the γ1 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.

AB - 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 γ1 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 γ1-AMPK. In addition we found that plectin affects the subunit composition of AMPK, because isoform α1 of the catalytic subunit decreased in proportion to isoform α2 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 α1-γ1 AMPK complexes by binding to the γ1 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.

KW - AMPK regulation

KW - Cytolinker proteins

KW - Cytoskeleton

KW - Myoblast differentiation

KW - Z-lines

UR - http://www.scopus.com/inward/record.url?scp=33744541891&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33744541891&partnerID=8YFLogxK

U2 - 10.1242/jcs.02891

DO - 10.1242/jcs.02891

M3 - Article

C2 - 16608880

AN - SCOPUS:33744541891

VL - 119

SP - 1864

EP - 1875

JO - Journal of Cell Science

JF - Journal of Cell Science

SN - 0021-9533

IS - 9

ER -