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Focal adhesion kinase and its role in skeletal muscle

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Abstract

Skeletal muscle has a remarkable ability to respond to different physical stresses. Loading muscle through exercise, either anaerobic or aerobic, can lead to increases in muscle size and function while, conversely, the absence of muscle loading stimulates rapid decreases in size and function. A principal mediator of this load-induced change is focal adhesion kinase (FAK), a downstream non-receptor tyrosine kinase that translates the cytoskeletal stress and strain signals transmitted across the cytoplasmic membrane by integrins to activate multiple anti-apoptotic and cell growth pathways. Changes in FAK expression and phosphorylation have been found to correlate to specific developmental states in myoblast differentiation, muscle fiber formation and muscle size in response to loading and unloading. With the capability to regulate costamere formation, hypertrophy and glucose metabolism, FAK is a molecule with diverse functions that are important in regulating muscle cell health.

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Abbreviations

FAK:

Focal adhesion kinase

PI3K:

Phosphatidylinositol-3 kinase

ERK1/2:

Extracellular signal-related kinase 1/2

mTOR:

Mechanistic target of rapamycin

SCI:

Spinal cord injury

PKC:

Protein kinase C

ECM:

Extracellular matrix

IGF-1:

Insulin-like growth factor 1

FERM:

4.1 ezrin, radixin, moesin domain

FAT:

Focal adhesion targeting

MDB2:

Methyl CpG-binding protein 2

FRNK:

Focal adhesion kinase-related non-kinase (FRNK)

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Acknowledgments

This work was supported by a Veterans Affairs Rehabilitation Research and Development Service grant (B9212C) and the James J. Peters VA Medical Center, where Dr. Cardozo is a member of the Medical-Surgical Service and Dr. Graham is a member of the Research Service.

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Correspondence to Christopher P. Cardozo.

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Graham, Z.A., Gallagher, P.M. & Cardozo, C.P. Focal adhesion kinase and its role in skeletal muscle. J Muscle Res Cell Motil 36, 305–315 (2015). https://doi.org/10.1007/s10974-015-9415-3

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  • DOI: https://doi.org/10.1007/s10974-015-9415-3

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