Calpain 1-gamma filamin interaction in muscle cells: a possible in situ regulation by PKC-alpha
| Autor: | Fabrice, Raynaud, Raynaud, Fabrice, Carole, Jond-Necand, Jond-Necand, Carole, Anne, Marcilhac, Marcilhac, Anne, Dieter, Fürst, Fürst, Dieter, Yves, Benyamin, Benyamin, Yves |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
animal structures
Protein Kinase C-alpha Proteolysis Filamins macromolecular substances Filamin Biochemistry Mice Contractile Proteins Chlorocebus aethiops medicine Myocyte Animals Humans Protein Isoforms Muscle Skeletal Protein kinase C Cells Cultured Sarcolemma Binding Sites medicine.diagnostic_test biology Myogenesis Calpain Microfilament Proteins Cell Biology Cell biology Protein Structure Tertiary body regions COS Cells biology.protein Phosphorylation Calcium Cattle Chickens |
| Zdroj: | The international journal of biochemistrycell biology. 38(3) |
| ISSN: | 1357-2725 |
| Popis: | Calpains are a family of calcium-dependent cysteine-proteases involved in cytoskeleton remodelling and muscle differentiation. In a recent study, we observed the presence of calpain 1 in the muscle contractile apparatus and specifically in the N1- and N2-lines. 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 1 substrate and to characterise this interaction. Gamma-filamin is a major muscle architectural protein located in the Z-line 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 1 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 1 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 1 in COS cells. Stimulation of PKC activity in myotubes, prevented gamma-filamin proteolysis by calpain and resulted in an increase in myotube adhesion. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect