Activating Compound | Comment | Organism | Structure |
---|---|---|---|
staurosporine | in myotubes, staurosporine increases proteasome activity by 38% and stimulates cleavage of proteasome subunits, Rpt2, Rpt6, and Rpn2. Rpt5 and Rpn10 subunits are not cleaved in staurosporine-treated myotubes | Mus musculus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
DEVD-CHO | a potent caspase-3 inhibitor | Mus musculus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
19 S proteasome + H2O | Mus musculus | caspase-3 specifically cleaves the 19 S component of 26 S proteasome Rpt2, Rpt6, and Rpn2 in skeletal muscle stimulating proteasome activity | ? | - |
? | |
Rpt2 + H2O | Mus musculus | - |
? | - |
? | |
Rpt5 + H2O | Mus musculus | in myoblasts, Rpt5 is sensitive to caspase-3-induced cleavage but in myotubes, it is not sensitive. Caspase-3 cleavage of Rpt5 is responsible for the difference in the patterns of proteasome subunit cleavage in myoblasts compared with myotubes | ? | - |
? | |
Rpt6 + H2O | Mus musculus | - |
? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
C2C12 cell | - |
Mus musculus | - |
heart | - |
Mus musculus | - |
myoblast | - |
Mus musculus | - |
myotube | - |
Mus musculus | - |
skeletal muscle | during differentiation of myoblasts to myotubes, there is an obligatory, transient increase in caspase-3 activity, accompanied by a corresponding increase in proteasome activity and cleavage of Rpt2 and Rpt6 | Mus musculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
19 S proteasome + H2O | - |
Mus musculus | ? | - |
? | |
19 S proteasome + H2O | caspase-3 specifically cleaves the 19 S component of 26 S proteasome Rpt2, Rpt6, and Rpn2 in skeletal muscle stimulating proteasome activity | Mus musculus | ? | - |
? | |
LLVY-4-methylcoumarin 7-amide + H2O | - |
Mus musculus | LLVY + 7-amino-4-methylcoumarin | - |
? | |
additional information | the caspase-3 cleavage site is present within the ATPase domain of Rpt subunits | Mus musculus | ? | - |
? | |
Rpt2 + H2O | - |
Mus musculus | ? | - |
? | |
Rpt5 + H2O | - |
Mus musculus | ? | - |
? | |
Rpt5 + H2O | in myoblasts, Rpt5 is sensitive to caspase-3-induced cleavage but in myotubes, it is not sensitive. Caspase-3 cleavage of Rpt5 is responsible for the difference in the patterns of proteasome subunit cleavage in myoblasts compared with myotubes | Mus musculus | ? | - |
? | |
Rpt6 + H2O | - |
Mus musculus | ? | - |
? |
General Information | Comment | Organism |
---|---|---|
malfunction | in mice with a muscle wasting condition, chronic kidney disease, occurs cleavage of subunits Rpt2 and Rpt6 and stimulation of proteasome activity | Mus musculus |
metabolism | the stage of muscle cell differentiation determines not only the caspase-3-induced subunit cleavage patterns but also the changes in proteasome activity | Mus musculus |
physiological function | caspase-3 cleaves specific 19 S proteasome subunits in skeletal muscle stimulating proteasome activity. Caspase-3 increases proteasome activity in myotubes but not in myoblasts by cleaving Rpt2 and Rpt6, while in myoblasts, caspase-3 cleaves Rpt5 to decrease proteasome activity, a feed-forward amplification that augments muscle proteolysis in catabolic conditions, overview | Mus musculus |