Subcellular localization and in vivo subunit interactions of ubiquitous mu-calpain.

@article{GilParrado2003SubcellularLA,
  title={Subcellular localization and in vivo subunit interactions of ubiquitous mu-calpain.},
  author={Shirley Gil-Parrado and O. Popp and Tobias A. Knoch and Stefan Zahler and Felix Bestvater and Marcel Felgentr{\"a}ger and Andreas Holloschi and Amaury Fern{\'a}ndez-Montalv{\'a}n and Ennes A. Auerswald and Hans Fritz and Pablo Fuentes-Prior and Werner Machleidt and Eberhard Spiess},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 18},
  pages={16336-46}
}
Ubiquitously expressed calpains are Ca(2+)-dependent, intracellular cysteine proteases comprising a large catalytic subunit (domains DI-DIV) and a noncovalently bound small regulatory subunit (domains DV and DVI). It is unclear whether Ca(2+)-induced calpain activation is followed by subunit dissociation or not. Here, we have applied advanced fluorescence microscopy techniques to study calpain subunit interactions in living cells using recombinant calpain subunits or domains fused to enhanced… CONTINUE READING

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