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Displays phosphatase activity for serine/threonine residues, and, dephosphorylates and activates MAP3K5 kinase. Additionally we are shipping PGAM5 Antibodies (4) and PGAM5 Kits (3) and many more products for this protein.
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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 (show PINK1 Proteins) pathway related to maintenance of the mitochondria.
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 (show RIPK3 Proteins)-PGAM5-Drp1 (show CRMP1 Proteins)/NFAT (show NFATC1 Proteins) signalling in NKT (show SLC22A6 Proteins) cell activation, and further suggest that RIPK3 (show RIPK3 Proteins)-PGAM5 signalling may mediate crosstalk between mitochondrial function and immune signalling.
The BCL2L1 (show BCL2L1 Proteins)-PGAM5-FUNDC1 (show FUNDC1 Proteins) axis is critical for receptor-mediated mitophagy.
Dephosphorylation of FUNDC1 (show FUNDC1 Proteins) by PGAM5 induces mitophagy.
PGAM5 is proteolytically processed, accumulates in the cytosol during apoptosis, and sensitizes cells to death.
Rhomboid protease PARL (show PARL Proteins) mediates the mitochondrial membrane potential loss-induced cleavage of PGAM5.
Experimental data indicate that the two splice variants of the mitochondrial protein (show COX6B2 Proteins) 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 (show KEAP1 Proteins).
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 (show MAP3K5 Proteins).
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 (show RALBP1 Proteins)/RIP3 to mediate necroptosis. Instead, PGAM5 protects cells from necroptosis by independently promoting mitophagy.
PGAM5 is a novel regulator of inflammasome and caspase 1 (show CASP1 Proteins) activity that functions independently of RIPK3 (show RIPK3 Proteins).
Results identify a crucial role for RIPK3 (show RIPK3 Proteins)-PGAM5-Drp1 (show CRMP1 Proteins)/NFAT (show NFATC1 Proteins) signalling in NKT (show CTSL1 Proteins) cell activation, and further suggest that RIPK3 (show RIPK3 Proteins)-PGAM5 signalling may mediate crosstalk between mitochondrial function and immune signalling.
Loss of PGAM5 disables PINK1 (show PINK1 Proteins)-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.
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