anti-ClpP Caseinolytic Peptidase, ATP-Dependent, Proteolytic Subunit Homolog (E. Coli) (CLPP) Antibodies

Mouse (Murine) ClpP Caseinolytic Peptidase, ATP-Dependent, Proteolytic Subunit Homolog (E. Coli) (CLPP) interaction partners

1. Loss of the mitochondrial matrix protease CLPP results in a lean phenotype with improved glucose homeostasis. Whole-body CLPP-deficient mice are protected from diet-induced obesity and insulin resistance. CLPP ablation also leads to a decline in brown adipocytes function leaving mice unable to cope with a cold-induced stress due to non-functional adaptive thermogenesis.

2. Our results show that absence of ClpP triggers compensatory responses in mice and suggest that ClpP might be dispensable for mammalian UPR(mt) initiation. Thus, we made an unexpected finding that deficiency of ClpP in mice is metabolically beneficial

3. we demonstrate that a strong mitochondrial cardiomyopathy and diminished respiration due to DARS2 deficiency can be alleviated by the loss of CLPP, leading to an increased de novo synthesis of individual OXPHOS subunits.

4. The authors present evidence that mammalian CLPP has an essential role in determining the rate of mitochondrial protein synthesis by regulating the level of mitoribosome assembly.

5. Novel effects of ClpP on mitochondrial morphology, cell proliferation and protein translation pathways in muscle cells.

6. Loss of mitochondrial peptidase Clpp leads to infertility, hearing loss plus growth retardation via accumulation of CLPX, mtDNA and inflammatory factors.

7. The correlative effect of Lon and ClpP upregulation on loss of mitochondrial Fe-S proteins during the progression of the disease may suggest that Fe-S proteins are potential targets of Lon and ClpP proteases in FRDA.

Human ClpP Caseinolytic Peptidase, ATP-Dependent, Proteolytic Subunit Homolog (E. Coli) (CLPP) interaction partners

1. Mitochondrial overexpression of human ClpP protects HeLa cells from killing by cisplatin. Overexpression of human ClpP desensitizes cells to cisplatin.

2. Autophagy compensates impaired energy metabolism in CLPXP-deficient Podospora anserina strains and extends healthspan.

3. we demonstrate that a strong mitochondrial cardiomyopathy and diminished respiration due to DARS2 deficiency can be alleviated by the loss of CLPP, leading to an increased de novo synthesis of individual OXPHOS subunits.

4. ere we present eight families affected by Perrault syndrome. In five families we identified novel or previously reported variants in HSD17B4, LARS2, CLPP and C10orf2

5. Data suggest that tumors exploit ClpXP-directed proteostasis to maintain mitochondrial bioenergetics, buffer oxidative stress, and enable metastatic competence.

6. Data indicate endopeptidase Clp (ClpP) mutation identified in two patients with Perrault syndrome type 3 in a Turkish family.

7. ClpP proteases from E. coli, S. aureus, and human mitochondria exhibit preferences for certain amino acids in the P1, P2, and P3 positions .

8. Optical trapping to assay single-molecule ClpXP unfolding and translocation of substrates consisting of domains with varying stabilities and sequences; find that ClpXP unfolds most domains by a single pathway, with kinetics that depend on the native fold and structural stability.

9. Deletion of PaClpP, leads to an unexpected healthy phenotype and increased lifespan of the fungal ageing model organism Podospora anserina and This phenotype can be reverted by expression of human ClpP.

10. Perrault syndrome is caused by recessive mutations in CLPP.

11. the N-terminal peptide of ClpP is a structural component of the substrate translocation channel and may play an important functional role as well

12. hClpX can regulate the appearance of hClpP peptidase activity in mitochondria and might affect the nature of the degradation products released during ATP-dependent proteolytic cycles

13. We propose that decreased levels of mitochondrial proteases Lon and ClpP may allow heat shock protein 60 substrate proteins to go through more folding attempts