@article{RaynaudJondNecandMarcilhacetal.2006,
  author    = {Raynaud, F and Jond-Necand, C and Marcilhac, Anne and F{\"u}rst, Dieter Oswald and Benyamin, Yves},
  title     = {Calpain 1-gamma filamin interaction in muscle cells : a possible in situ regulation by PKC-alpha},
  year      = {2006},
  language  = {en}
}
@article{RaynaudJondNecandMarcilhacetal.2006,
  author    = {Raynaud, F and Jond-Necand, C and Marcilhac, Anne and F{\"u}rst, Dieter Oswald and Benyamin, Yves},
  title     = {Calpain 1-gamma filamin interaction in muscle cells :a possible in situ regulation by PKC-alpha},
  year      = {2006},
  language  = {en}
}
@article{RaynaudJondNecandMarcilhacetal.2006,
  author    = {Raynaud, Fabrice and Jond-Necand, Carole and Marcilhac, Anne and F{\"u}rst, Dieter and Benyamin, Yves},
  title     = {Calpain 1-gamma filamin interaction in muscle cells : a possible in situ regulation by PKC-alpha},
  issn      = {1357-2725},
  doi       = {10.1016/j.biocel.2005.09.020},
  year      = {2006},
  abstract  = {Calpains are a family of calcium-dependant cysteine-proteases involved in cytoskeleton remodelling and muscle differentiation. In a recent study, we observed the presence of calpain I in the muscle contractile apparatus and specifically in the N1- and N2-fines. This calpain isoform was found to be involved in the degradation of muscle fibres via proteolysis of key proteins in Z-disk and costameric junctions. The goal of this study was to determine whether gamma-filamin - a specific muscle isoform of the filamin family - is a calpain, I substrate and to characterise this interaction. gamma-Filamin is a major muscle architectural protein located in the Z-fine and under the sarcolemmal membrane. This protein is a component of the chain binding the sarcolemma to the sarcomeric structure. In this study, we found that gamma-filamin formed a stable complex in vitro and in cells with calpain I in the absence of calcium stimulation. We also located the binding domains in the C-terminus of gamma-filamin with a cleavage site between serine 2626 and serine 2627 in the hinge 2 region. The catalytic (80 kDa) and regulatory (28 kDa) subunits of calpain I are both involved in high affinity binding at gamma-filamin. Moreover, we showed that phosphorylation of the filamin C- terminus domain by PKC alpha protected gamma-filamin against proteolysis by calpain I in COS cells. Stimulation of PKC activity in myotubes, prevented gamma-filamin proteolysis by calpain and resulted in an increase in myotube adhesion.},
  language  = {en}
}