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Displays phosphatase activity for serine/threonine residues, and, dephosphorylates and activates MAP3K5 kinase. Zusätzlich bieten wir Ihnen PGAM5 Antikörper (10) und PGAM5 Kits (9) und viele weitere Produktgruppen zu diesem Protein an.
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The authors show that developmental mitochondrial unfolded protein response is necessary and sufficient to extend Drosophila lifespan, and identify Phosphoglycerate Mutase 5 (PGAM5) as a mediator of this response. Developmental mitochondrial stress leads to activation of FoxO, via Apoptosis Signal-regulating Kinase 1 (ASK1) and Jun-N-terminal Kinase (JNK).
the mushroom body may possess an apoptosis-dependent toxic function, the suppression of which by dPGAM5 appears to be crucial for heat shock resistance.
PGAM5 negatively regulates the PINK1 pathway related to maintenance of the mitochondria.
An intact complex of PGAM5-KEAP1-Nrf2 preserves mitochondrial motility by suppressing dominant-negative KEAP1 activity.
PGAM5 regulates histidine phosphorylation to control TCR activation of CD4-positive T cells.
Results indicate that a multiprotein complex including PGAM5, Bax and Drp1 proteins specifically formed during intrinsic apoptosis induction.
Results identify a crucial role for RIPK3-PGAM5-Drp1/NFAT signalling in NKT cell activation, and further suggest that RIPK3-PGAM5 signalling may mediate crosstalk between mitochondrial function and immune signalling.
The BCL2L1-PGAM5-FUNDC1 axis is critical for receptor-mediated mitophagy.
Dephosphorylation of FUNDC1 by PGAM5 induces mitophagy.
PGAM5 is proteolytically processed, accumulates in the cytosol during apoptosis, and sensitizes cells to death.
Rhomboid protease PARL mediates the mitochondrial membrane potential loss-induced cleavage of PGAM5.
Experimental data indicate that the two splice variants of the mitochondrial protein phosphatase PGAM5 are at the convergent point of multiple necrosis pathways.
The N terminus of the PGAM5 protein contains a conserved NXESGE motif that binds to the substrate binding pocket in the Kelch domain of Keap1.
Results suggest that this member of the PGAM family has crossed over from small molecules to protein substrates and been adapted to serve as a specialized activator of ASK1.
melatonin treatment inhibited the Ripk3-PGAM5-CypD-mPTP cascade and thus reduced cellular necroptosis, conferring a protective advantage to the endothelial system in IR stress.
findings suggest that HO-1 protects against I/R-induced hepatic injury via regulation of mitochondrial QC by PGAM5 signaling.
Taken together, our findings provide evidence that NBP can attenuate the progression of EAE by suppressing PGAM5-induced necroptosis and inflammation in microglia and represents a new therapeutic strategy for treating autoimmune diseases.
Results revealed that RIPK1 and PGAM5 function independently to exert optimal control of Leishmania replication in the host.
Our data demonstrate for the first time that PGAM5 plays an indispensable role in the pathogenesis of ConA-induced liver injury.
we also found that Pgam5-deficient mice are resistant to high-fat-diet-induced obesity. Our study uncovered that PGAM5 is involved in the whole-body metabolism in response to stresses that impose metabolic challenges on mitochondria.
Our results revise the former proposal that PGAM5 acts downstream of RIP1/RIP3 to mediate necroptosis. Instead, PGAM5 protects cells from necroptosis by independently promoting mitophagy.
PGAM5 is a novel regulator of inflammasome and caspase 1 activity that functions independently of RIPK3.
Loss of PGAM5 disables PINK1-mediated mitophagy in vitro and leads to dopaminergic neurodegeneration and mild dopamine loss in vivo causing a Parkinson's-like movement disorder.
Data indicate that phosphoglycerate mutase 5 (PGAM5) contains an N-terminal WDXNWD motif required for multimerization and maximal phosphatase activity.
Pgam5 is essential for head formation, and for establishing and maintaining the Wnt/beta-Catenin signaling gradient that patterns the anterior-posterior body axis. We show that Pgam5 interacts with Dishevelled2 and that Dishevelled2 is a substrate of Pgam5.
Displays phosphatase activity for serine/threonine residues, and, dephosphorylates and activates MAP3K5 kinase. Has apparently no phosphoglycerate mutase activity. May be regulator of mitochondrial dynamics. Substrate for a KEAP1-dependent ubiquitin ligase complex. Contributes to the repression of NFE2L2- dependent gene expression (By similarity).
, phosphoglycerate mutase 5
, Bcl-XL-binding protein v68
, serine/threonine-protein phosphatase PGAM5, mitochondrial