ZAKβ is activated by cellular compression and mediates contraction-induced MAP kinase signaling in skeletal muscle.
ZAKβ
mechanobiology
muscle contraction
myopathy
Journal
The EMBO journal
ISSN: 1460-2075
Titre abrégé: EMBO J
Pays: England
ID NLM: 8208664
Informations de publication
Date de publication:
01 09 2022
01 09 2022
Historique:
revised:
28
05
2022
received:
12
05
2022
accepted:
22
06
2022
pubmed:
29
7
2022
medline:
9
9
2022
entrez:
28
7
2022
Statut:
ppublish
Résumé
Mechanical inputs give rise to p38 and JNK activation, which mediate adaptive physiological responses in various tissues. In skeletal muscle, contraction-induced p38 and JNK signaling ensure adaptation to exercise, muscle repair, and hypertrophy. However, the mechanisms by which muscle fibers sense mechanical load to activate this signaling have remained elusive. Here, we show that the upstream MAP3K ZAKβ is activated by cellular compression induced by osmotic shock and cyclic compression in vitro, and muscle contraction in vivo. This function relies on ZAKβ's ability to recognize stress fibers in cells and Z-discs in muscle fibers when mechanically perturbed. Consequently, ZAK-deficient mice present with skeletal muscle defects characterized by fibers with centralized nuclei and progressive adaptation towards a slower myosin profile. Our results highlight how cells in general respond to mechanical compressive load and how mechanical forces generated during muscle contraction are translated into MAP kinase signaling.
Identifiants
pubmed: 35899396
doi: 10.15252/embj.2022111650
pmc: PMC9434084
doi:
Substances chimiques
Mitogen-Activated Protein Kinases
EC 2.7.11.24
p38 Mitogen-Activated Protein Kinases
EC 2.7.11.24
MAP Kinase Kinase Kinases
EC 2.7.11.25
ZAK protein, mouse
EC 2.7.11.25
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e111650Informations de copyright
© 2022 The Authors. Published under the terms of the CC BY NC ND 4.0 license.
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