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Displays phosphatase activity for serine/threonine residues, and, dephosphorylates and activates MAP3K5 kinase. Zusätzlich bieten wir Ihnen PGAM5 Antikörper (8) und PGAM5 Proteine (7) und viele weitere Produktgruppen zu diesem Protein an.
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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 pathway related to maintenance of the mitochondria.
PGAM5 regulates histidine phosphorylation to control TCR activation of CD4 (zeige CD4 ELISA Kits)-positive T cells.
Results indicate that a multiprotein complex including PGAM5, Bax (zeige BAX ELISA Kits) and Drp1 (zeige CRMP1 ELISA Kits) proteins specifically formed during intrinsic apoptosis induction.
Results identify a crucial role for RIPK3 (zeige RIPK3 ELISA Kits)-PGAM5-Drp1 (zeige CRMP1 ELISA Kits)/NFAT (zeige NFATC1 ELISA Kits) signalling in NKT (zeige SLC22A6 ELISA Kits) cell activation, and further suggest that RIPK3 (zeige RIPK3 ELISA Kits)-PGAM5 signalling may mediate crosstalk between mitochondrial function and immune signalling.
The BCL2L1 (zeige BCL2L1 ELISA Kits)-PGAM5-FUNDC1 (zeige FUNDC1 ELISA Kits) axis is critical for receptor-mediated mitophagy.
Dephosphorylation of FUNDC1 (zeige FUNDC1 ELISA Kits) by PGAM5 induces mitophagy.
PGAM5 is proteolytically processed, accumulates in the cytosol during apoptosis, and sensitizes cells to death.
Rhomboid protease PARL (zeige PARL ELISA Kits) mediates the mitochondrial membrane potential loss-induced cleavage of PGAM5.
Experimental data indicate that the two splice variants of the mitochondrial protein (zeige COX6B2 ELISA Kits) 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 (zeige KEAP1 ELISA Kits).
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 (zeige MAP3K5 ELISA Kits).
Results revealed that RIPK1 (zeige RIPK1 ELISA Kits) 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 (zeige RALBP1 ELISA Kits)/RIP3 (zeige MPRIP ELISA Kits) to mediate necroptosis. Instead, PGAM5 protects cells from necroptosis by independently promoting mitophagy.
PGAM5 is a novel regulator of inflammasome and caspase 1 (zeige CASP1 ELISA Kits) activity that functions independently of RIPK3 (zeige RIPK3 ELISA Kits).
Results identify a crucial role for RIPK3 (zeige RIPK3 ELISA Kits)-PGAM5-Drp1 (zeige CRMP1 ELISA Kits)/NFAT (zeige NFATC1 ELISA Kits) signalling in NKT (zeige CTSL1 ELISA Kits) cell activation, and further suggest that RIPK3 (zeige RIPK3 ELISA Kits)-PGAM5 signalling may mediate crosstalk between mitochondrial function and immune signalling.
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 (zeige WNT2 ELISA Kits)/beta-Catenin (zeige CTNNB1 ELISA Kits) 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