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Phosphatidylinositol transfer protein, alpha

PITPalpha, Phosphatidylinositol transfer protein, Phosphatidylinositol transfer protein alpha
catalyzes the transfer of phosphatidylinositol (PtdIns) between membranes [RGD, Feb 2006] (from NCBI)
Top mentioned proteins: PITPbeta, CAN, ACID, PLC, HAD
Papers on PITPalpha
Phosphatidylinositol transfer protein, cytoplasmic 1 (PITPNC1) binds and transfers phosphatidic acid.
Cockcroft et al., London, United Kingdom. In J Biol Chem, 2012
The best characterized mammalian PITPs are the Class I PITPs, PITPα (PITPNA) and PITPβ (PITPNB), which are single domain proteins with a hydrophobic cavity that binds a phosphatidylinositol (PI) or phosphatidylcholine molecule.
Modifier genes for mouse phosphatidylinositol transfer protein α (vibrator) that bypass juvenile lethality.
Hamilton et al., San Diego, United States. In Genetics, 2011
These results indicate a mechanism of suppression that bypasses a quantitative requirement for PITPalpha function.
Proteome analysis of the thalamus and cerebrospinal fluid reveals glycolysis dysfunction and potential biomarkers candidates for schizophrenia.
Turck et al., München, Germany. In J Psychiatr Res, 2010
This protein has been found differentially expressed in thalami from patients with schizophrenia.
Zebrafish class 1 phosphatidylinositol transfer proteins: PITPbeta and double cone cell outer segment integrity in retina.
Bankaitis et al., Chapel Hill, United States. In Traffic, 2010
Zebrafish express PITPalpha and PITPbeta-isoforms (Pitpna and Pitpnb, respectively) and a novel PITPbeta-like isoform (Pitpng).
Phosphatidylinositol- and phosphatidylcholine-transfer activity of PITPbeta is essential for COPI-mediated retrograde transport from the Golgi to the endoplasmic reticulum.
Cockcroft et al., London, United Kingdom. In J Cell Sci, 2010
Phosphatidylinositol transfer protein beta (PITPbeta), an essential protein that possesses phosphatidylinositol (PtdIns) and phosphatidylcholine (PtdCho) lipid transfer activity is known to localise to the Golgi and ER but its role in these membrane systems is not clear.
The anti-apoptotic activity associated with phosphatidylinositol transfer protein alpha activates the MAPK and Akt/PKB pathway.
Snoek et al., Utrecht, Netherlands. In Biochim Biophys Acta, 2008
The conditioned medium (CM) from mouse NIH3T3 fibroblast cells overexpressing phosphatidylinositol transfer protein alpha (PI-TPalpha; SPIalpha cells) demonstrates an increased anti-apoptotic activity compared with CM from wild type NIH3T3 (wtNIH3T3) cells.
Dynamics of lipid transfer by phosphatidylinositol transfer proteins in cells.
Cockcroft et al., London, United Kingdom. In Traffic, 2008
Among these, phosphatidylinositol transfer proteins (PITP) are of particular interest as they can bind to and transfer phosphatidylinositol (PtdIns)--the precursor of important signalling molecules, phosphoinositides--and because they have essential functions in neuronal development (PITPalpha) and cytokinesis (PITPbeta).
Regulation of PI3K signalling by the phosphatidylinositol transfer protein PITPalpha during axonal extension in hippocampal neurons.
Eickholt et al., London, United Kingdom. In J Cell Sci, 2008
Here, we show that PITPalpha is enriched in specific areas of the postnatal and adult brain, including the hippocampus and cerebellum.
The pathologies associated with functional titration of phosphatidylinositol transfer protein alpha activity in mice.
Bankaitis et al., Chapel Hill, United States. In J Lipid Res, 2007
phosphatidylinositol binding is an essential functional property of PITPalpha in vivo, and suggest a causal linkage between defects in lipid transport and glucose homeostasis and cerebellar inflammatory disease
Biochemical and biological functions of class I phosphatidylinositol transfer proteins.
Carvou et al., London, United Kingdom. In Biochim Biophys Acta, 2007
Mammalian phosphatidylinositol transfer proteins, PITPalpha and PITPbeta are paralogs that share 77% sequence identity and contain a hydrophobic cavity that can sequester either phosphatidylinositol or phosphatidylcholine.
RdgB proteins: functions in lipid homeostasis and signal transduction.
Padinjat et al., Cambridge, United Kingdom. In Biochim Biophys Acta, 2007
The RdgBs are a group of evolutionarily conserved molecules that contain a phosphatidylinositol transfer protein (PITP) domain.
Violating the splicing rules: TG dinucleotides function as alternative 3' splice sites in U2-dependent introns.
Platzer et al., Jena, Germany. In Genome Biol, 2006
the apparent occurrence of an unusual TG 3' splice site in intron 4 is discussed
Trafficking of phosphatidylinositol by phosphatidylinositol transfer proteins.
Cockcroft, London, United Kingdom. In Biochem Soc Symp, 2006
Mammalian PITPs, PITPalpha and PITPbeta, are paralogous genes that are 94% similar in sequence.
Phosphatidylinositol transfer protein expression altered by aging and Parkinson disease.
Strosznajder et al., Warsaw, Poland. In Cell Mol Neurobiol, 2006
Lower protein expression of PI-TP(alpha and beta) in aged brain and in PD.
Phosphatidylinositol transfer protein-alpha in netrin-1-induced PLC signalling and neurite outgrowth.
Xiong et al., Augusta, United States. In Nat Cell Biol, 2005
These results identify a crucial role for PlTPalpha in netrin-1-induced neurite outgrowth, revealing a signalling mechanism for DCC/neogenin and PlTPalpha regulation.
Phosphatidylinositol transfer protein function in the yeast Saccharomyces cerevisiae.
Xie et al., Chapel Hill, United States. In Adv Enzyme Regul, 2004
PITPs regulate the interface between lipid metabolism and cellular functions, but the fundamental nature of this regulation is not understood.
Structure-function relationships of phosphatidylinositol transfer proteins: involvement of phosphorylation sites.
Egmond et al., Utrecht, Netherlands. In Biochimie, 2004
The mammalian low molecular weight phosphatidylinositol transfer proteins: PI-TPalpha and PI-TPbeta are extremely well conserved and highly homologous.
The Role of Phosphatidylinositol Transfer Proteins (PITPs) in Intracellular Signalling.
Cockcroft et al., London, United Kingdom. In Trends Endocrinol Metab, 1998
Phosphatidylinositol transfer protein (PITP) has been identified as a key player in numerous signalling pathways relying on phosphatidylinositol (PI) metabolites.
Phosphatidylinositol transfer protein required for ATP-dependent priming of Ca(2+)-activated secretion.
Martin et al., Madison, United States. In Nature, 1994
Here we show that one of the mammalian priming factors (PEP3) is identical to phosphatidylinositol transfer protein (PITP).
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