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Phospholipid scramblase 3

phospholipid scramblase 3, PLSCR3, hPLSCR3
Top mentioned proteins: T-plastin, ACID, V1a, ALG-2, CAN
Papers on phospholipid scramblase 3
Tubby-like protein superfamily member PLSCR3 functions as a negative regulator of adipogenesis in mouse 3T3-L1 preadipocytes by suppressing induction of late differentiation stage transcription factors.
Maki et al., Nagoya, Japan. In Biosci Rep, Jan 2016
UNASSIGNED: PLSCR3 (phospholipid scramblase 3, Scr3) belongs to the superfamily of membrane-associated transcription regulators named Tubby-like proteins (TULPs).
Cardiolipin externalization to the outer mitochondrial membrane acts as an elimination signal for mitophagy in neuronal cells.
Kagan et al., Pittsburgh, United States. In Nat Cell Biol, 2013
RNAi knockdown of cardiolipin synthase or of phospholipid scramblase-3, which transports cardiolipin to the outer mitochondrial membrane, decreased the delivery of mitochondria to autophagosomes.
The effects of chronic muscle use and disuse on cardiolipin metabolism.
Hood et al., Toronto, Canada. In J Appl Physiol, 2013
To investigate the underlying mechanisms, we measured the mRNA expression of 1) CL synthesis enzymes cardiolipin synthase (CLS) and CTP:PA-cytidylyltransferase-1 (CDS-1); 2) remodeling enzymes tafazzin and acyl-CoA:lysocardiolipin acyltransferase-1 (ALCAT1); and 3) outer membrane CL enzymes, mitochondrial phospholipase D and phospholipid scramblase 3 (Plscr3), during chronic contractile activity (CCA)-induced mitochondrial biogenesis and denervation.
ALG-2-interacting Tubby-like protein superfamily member PLSCR3 is secreted by an exosomal pathway and taken up by recipient cultured cells.
Maki et al., Nagoya, Japan. In Biosci Rep, 2012
Using a previously established cell line of HEK-293 (human embryonic kidney-293) cells constitutively expressing human Scr3 (PLSCR3) that interacts with ALG-2 (apoptosis-linked gene 2) Ca²⁺-dependently, we found that Scr3 was secreted into the culture medium.
Prediction of a new ligand-binding site for type 2 motif based on the crystal structure of ALG-2 by dry and wet approaches.
Maki et al., Nagoya, Japan. In Int J Mol Sci, 2011
Two types of ALG-2-binding motifs have been determined: type 1, PXYPXnYP (X, variable; n = 4), in ALIX and PLSCR3; type 2, PXPGF, in Sec31A and PLSCR3.
Proteomic profiling of S-acylated macrophage proteins identifies a role for palmitoylation in mitochondrial targeting of phospholipid scramblase 3.
Fessler et al., United States. In Mol Cell Proteomics, 2011
Among the candidate novel S-acylproteins was phospholipid scramblase 3 (Plscr3), a protein that regulates apoptosis through remodeling the mitochondrial membrane.
Structure and function of ALG-2, a penta-EF-hand calcium-dependent adaptor protein.
Shibata et al., Nagoya, Japan. In Sci China Life Sci, 2011
With some exceptions, ALG-2-interacting proteins commonly contain Pro-rich regions, and ALG-2 recognizes at least two distinct Pro-containing motifs: PPYP(X)nYP (X, variable; n=4 in ALIX and PLSCR3) and PXPGF (represented by Sec31A).
Activation of protein kinase C delta following cerebral ischemia leads to release of cytochrome C from the mitochondria via bad pathway.
Perez-Pinzon et al., Miami, United States. In Plos One, 2010
We tested two potential pathways by which δPKC activation could lead to cytochrome c release: phosphorylation of phospholipid scramblase-3 (PLSCR3) and/or protein phosphatase 2A (PP2A).
The dynamics of cardiolipin synthesis post-mitochondrial fusion.
Hatch et al., Winnipeg, Canada. In Biochim Biophys Acta, 2010
In addition, Mfn-2 expression was not altered in Hela cells expressing phospholipid scramblase-3 or a disrupted scramblase indicating that proper CL localization within mitochondria is not essential for Mfn-2 expression.
Hyperthermia-induced apoptosis in Tca8113 cells is inhibited by heat shock protein 27 through blocking phospholipid scramblase 3 phosphorylation.
He et al., Kunming, China. In Int J Hyperthermia, 2009
Phospholipid scramblase 3 (PLS3), a target of protein kinase C-delta (PKC-delta), resides in mitochondria and plays pivotal roles in regulating apoptotic response.
Calcium binding studies of peptides of human phospholipid scramblases 1 to 4 suggest that scramblases are new class of calcium binding proteins in the cell.
Gummadi et al., Chennai, India. In Biochim Biophys Acta, 2009
Results show that binding affinities of the peptides are in the order hPLSCR1>hPLSCR3>hPLSCR2>hPLSCR4 for Ca2+ and in the order hPLSCR1>hPLSCR2>hPLSCR3>hPLSCR4 for Mg2+.
Association of protein kinase C delta and phospholipid scramblase 3 in hippocampal mitochondria correlates with neuronal vulnerability to brain ischemia.
Zabłocka et al., Warsaw, Poland. In Neurochem Int, 2009
One of the targets of PKC delta is phospholipid scramblase 3 (PLSCR3), an enzyme responsible for cardiolipin translocation from the inner to outer mitochondrial membrane.
Tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL) induced mitochondrial pathway to apoptosis and caspase activation is potentiated by phospholipid scramblase-3.
Khosravi-Far et al., Boston, United States. In Apoptosis, 2008
TRAIL-induced activation of PKC-delta mediates regulation of the phospholipid scramblase3-induced changes in cardiolipin.
Role of phospholipid scramblase 3 in the regulation of tumor necrosis factor-alpha-induced apoptosis.
Lee et al., Salt Lake City, United States. In Biochemistry, 2008
We investigated the regulation of tBid-induced cytochrome c release and apoptosis by phospholipid scramblase 3 (PLS3).
Identification of Alix-type and Non-Alix-type ALG-2-binding sites in human phospholipid scramblase 3: differential binding to an alternatively spliced isoform and amino acid-substituted mutants.
Maki et al., Nagoya, Japan. In J Biol Chem, 2008
Identification of Alix-type and Non-Alix-type ALG-2-binding sites in human phospholipid scramblase 3: differential binding to an alternatively spliced isoform and amino acid-substituted mutants
[Protein kinases in mitochondria].
Zabłocka et al., Warsaw, Poland. In Postepy Biochem, 2007
Their role mainly concentrates at phosphorylation of pro- and anti-apoptotic proteins (Bad, Bax, Bcl-2, Bcl-xL), phosphorylation/modification of electron transport chain proteins (complex I, COIV), MPTP forming proteins VDAC and ANT, proteins of mitochondrial ATP-sensitive potassium channel (mitoK(ATP)) and phospholipid scramblase 3 (PLSCR3).
Phosphorylation of mitochondrial phospholipid scramblase 3 by protein kinase C-delta induces its activation and facilitates mitochondrial targeting of tBid.
Lee et al., Kunming, China. In J Cell Biochem, 2007
These findings indicate that phosphorylation of PLS3 by PKC-delta induces PLS3 activation to facilitate mitochondrial targeting of tBid and apoptosis.
Mobilization of pro-inflammatory lipids in obese Plscr3-deficient mice.
Siuzdak et al., Los Angeles, United States. In Genome Biol, 2006
identified previously unrecognized lipid metabolites that suggest a novel molecular link between obesity, inflammation and the downstream consequences associated with PLSCR3-deficiency
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