Myoblast migration is prevented by a calpain‐dependent accumulation of MARCKS

Dedieu, Stéphane; Mazères, Germain; Poussard, Sylvie; Brustis, Jean-Jacques; Cottin, Patrick

doi:10.1016/j.biolcel.2003.09.005

Cited by 44 publications

(44 citation statements)

References 79 publications

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“…In addition, human tumors overexpressing cyclin E have been associated with increased proteolysis of FAK (40). By contrast, in myoblasts overexpressing calpastatin, the proteolytic patterns of talin and FAK are unchanged, whereas an accumulation of MARCKS (myristoylated alanine-rich C kinase substrate) has been observed, indicating that calpain may preferentially cleave MARCKS to affect myoblast migration (41,42).…”

Section: Discussionmentioning

confidence: 99%

Regulation of Adhesion Dynamics by Calpain-mediated Proteolysis of Focal Adhesion Kinase (FAK)

Chan

Bennin

Huttenlocher

2010

Journal of Biological Chemistry

178

165

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The coordinated and dynamic regulation of adhesions is required for cell migration. We demonstrated previously that limited proteolysis of talin1 by the calcium-dependent protease calpain 2 plays a critical role in adhesion disassembly in fibroblasts ( The coordinated and dynamic regulation of adhesions is central for cell migration in both normal and pathological processes (1). Cell migration is initiated by forming protrusions, which are stabilized by integrin-mediated adhesions that establish structural and signaling linkages between the extracellular matrix and the actin cytoskeleton. Subsequently, actomyosin contractility drives forward propulsion, and finally, adhesions are disassembled to allow for directional movement. Thus, it is not surprising that efficient cell migration necessitates precise spatial and temporal control of these events. However, the mechanisms governing the formation and disassembly of adhesions are still not well understood.A prominent component involved in this regulation is focal adhesion kinase (FAK).2 FAK promotes cell migration by its capacity to orchestrate signals between integrin and growth factor receptors (2). Downstream of integrin or growth factor stimulation, FAK is phosphorylated at Tyr-397, which is an important binding site for Src family kinases (3). Previous studies have demonstrated a critical role for FAK as a regulator of adhesion dynamics (4 -7). In addition, FAK has been shown to mediate the tyrosine phosphorylation of p190RhoGAP as a negative regulator of Rho activity in focal adhesion turnover and polarity (5, 8). Furthermore, microtubule-induced focal adhesion disassembly requires FAK and dynamin (9). Nevertheless, the mechanisms by which FAK regulates the disassembly of focal adhesions remain to be elucidated. Evidence has emerged supporting the role of the calpain family of intracellular calcium-dependent proteases in regulating cell migration (10 -14). Calpains have been proposed to regulate migration, at least in part, through their ability to modulate the dynamics of adhesions (15). Numerous calpain targets have been identified, some of which are proteins that are present in focal adhesions, including talin, paxillin, and FAK (16). Thus, it is likely that proteolysis of these substrates contributes to the regulation of adhesion dynamics and cell migration.The involvement of both FAK and calpain in regulating the turnover of adhesions prompted us to investigate the cleavage of FAK by calpain as a possible mechanism by which FAK affects adhesion dynamics. We demonstrated previously that calpain-mediated proteolysis of talin regulates adhesion dynamics (17). Here, we show that FAK also regulates talin dynamics. We have identified the calpain cleavage site of FAK and have generated a mutant form of FAK that is resistant to calpain proteolysis. Expression of wild-type but not calpainresistant FAK restores the adhesion dynamics of talin in FAKdeficient cells. Taken together, our findings suggest a novel role for calpain-mediated cleavage of FAK in regulating...

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Section: Discussionmentioning

confidence: 99%

Regulation of Adhesion Dynamics by Calpain-mediated Proteolysis of Focal Adhesion Kinase (FAK)

Chan

Bennin

Huttenlocher

2010

Journal of Biological Chemistry

178

165

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“…Myoblast differentiation onto the cross-linked (PLL/HA) 12 films was then followed by analysis of the expression of muscle-specific proteins like myogenin and troponin T. For control surfaces, these proteins are known to be expressed after about 1-2 days in DM [33,34] and until at least day 6. Immunoblots of myogenin and troponin T expression at day 3 and day 6 in DM, for cells cultured on EDC30, EDC50 and EDC100 films are shown in Figure 6.…”

Section: Film Cross-linking Influences the Myogenic Differentiation Pmentioning

confidence: 99%

Polyelectrolyte Multilayer Films of Controlled Stiffness Modulate Myoblast Cell Differentiation

Ren

Crouzier

Roy

et al. 2008

Adv Funct Materials

244

263

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Beside chemical properties and topographical features, mechanical properties of gels have been recently demonstrated to play an important role in various cellular processes, including cell attachment, proliferation, and differentiation. In this work, we used multilayer films made of poly (L-lysine)/Hyaluronan (PLL/HA) of controlled stiffness to investigate the effects of mechanical properties of thin films on skeletal muscle cells (C2C12 cells) differentiation. Prior to differentiation, cells need to adhere and proliferate in growth medium. Stiff films (E 0 > 320 kPa) promoted formation of focal adhesions and organization of the cytoskeleton as well as an enhanced proliferation, whereas soft films were not favorable for cell anchoring, spreading or proliferation. Then C2C12 cells were switched to a low serum containing medium to induce cell differentiation, which was also greatly dependent on film stiffness. Although myogenin and troponin T expressions were only moderately affected by film stiffness, the morphology of the myotubes exhibited striking stiffness-dependent differences. Soft films allowed differentiation only for few days and the myotubes were very short and thick. Cell clumping followed by aggregates detachment could be observed after ~2 to 4 days. On stiffer films, significantly more elongated and thinner myotubes were observed for up to ~ 2 weeks. Myotube striation was also observed but only for the stiffer films. These results demonstrate that film stiffness modulates deeply adhesion, proliferation and differentiation, each of these processes having its own stiffness requirement.

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“…This system implicated in various physiological and pathological processes (Kidd et al, 2000;Huang et al, 2001;Goll et al, 2003;Raynaud et al, 2004) and involved in regulation of protein turn over and growth (Goll et al, 1992), myoblast migration (Dedieu et al, 2003) and fusion (Temm-Grove et al, 1999). CAST is therefore believed to be an excellent candidate gene for growth and carcass trait in livestocks.…”

Section: Introductionmentioning

confidence: 99%

Genetic Polymorphisms of the Coding Region (Exon 6) of Calpastatin in Indonesian Sheep

Dagong¹,

Sumantri²,

Noor³

et al. 2011

Med Pet

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Myoblast migration is prevented by a calpain‐dependent accumulation of MARCKS

Cited by 44 publications

References 79 publications

Regulation of Adhesion Dynamics by Calpain-mediated Proteolysis of Focal Adhesion Kinase (FAK)

Regulation of Adhesion Dynamics by Calpain-mediated Proteolysis of Focal Adhesion Kinase (FAK)

Polyelectrolyte Multilayer Films of Controlled Stiffness Modulate Myoblast Cell Differentiation

Genetic Polymorphisms of the Coding Region (Exon 6) of Calpastatin in Indonesian Sheep

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