Abstract |
p94/calpain 3, a skeletal muscle-specific member of calpain protease family, is characterized by apparent Ca(2+)-independence during exhaustive autolysis and concomitant proteolysis of non-self substrates. The purpose of our study was to comprehensively profile the structural basis of p94 enabling activation in the cytosol without an extra Ca(2+). Ca(2+)-dependent p94 mutants were screened using "p94-trapping", which is an application of yeast genetic reporter system called " proteinase-trapping". Several amino acids were revealed as critical for apparent Ca(2+)-independent p94 activity. These results highlight the importance of conserved amino acids in domain IIb as well as in the p94-specific IS2 region.
|
Authors | Yasuko Ono, Chikako Hayashi, Naoko Doi, Mai Tagami, Hiroyuki Sorimachi |
Journal | FEBS letters
(FEBS Lett)
Vol. 582
Issue 5
Pg. 691-8
(Mar 05 2008)
ISSN: 0014-5793 [Print] England |
PMID | 18258189
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
|
Chemical References |
- Muscle Proteins
- Mutant Proteins
- Sodium
- Peptide Hydrolases
- CAPN3 protein, human
- Calpain
- Calcium
|
Topics |
- Amino Acid Sequence
- Animals
- COS Cells
- Calcium
(pharmacology)
- Calpain
(chemistry, isolation & purification, metabolism)
- Chlorocebus aethiops
- Conserved Sequence
- Models, Molecular
- Molecular Sequence Data
- Muscle Proteins
(chemistry, isolation & purification, metabolism)
- Mutant Proteins
(chemistry, isolation & purification, metabolism)
- Mutation
(genetics)
- Peptide Hydrolases
(chemistry, metabolism)
- Protein Processing, Post-Translational
(drug effects)
- Protein Structure, Tertiary
- Sodium
(pharmacology)
- Structure-Activity Relationship
- Substrate Specificity
(drug effects)
|