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Phosphatidylinositol transfer protein, beta

The protein encoded by this gene is found in the cytoplasm, where it catalyzes the transfer of phosphatidylinositol and phosphatidylcholine between membranes. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: PITPalpha, CAN, ACID, HAD, Akt
Papers on PITPbeta
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.
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 and phosphatidylcholine exchange activity of PITPbeta is essential for COPI-mediated retrograde transport from the Golgi to the endoplasmic reticulum.
Measurement of phosphatidylinositol and phosphatidylcholine binding and transfer activity of the lipid transport protein PITP.
Cockcroft, London, United Kingdom. In Methods Mol Biol, 2008
In addition, PITPbeta can facilitate sphingomyelin transfer.
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.
Comparative proteomic analysis of peripheral blood mononuclear cells from atopic dermatitis patients and healthy donors.
Lee et al., Taejŏn, South Korea. In Bmb Rep, 2008
Significant changes were observed in the expressions of fourteen proteins, including the vinculin, PITPNB, and Filamin A proteins.
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).
In vivo dendritic cell depletion reduces breeding efficiency, affecting implantation and early placental development in mice.
Blois et al., Berlin, Germany. In J Mol Med (berl), 2008
In the present study, we were also able to identify a novel DC-dependent protein, phosphatidylinositol transfer protein beta (PITPbeta), involved in implantation and trophoblast development using a proteomic approach.
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
Overexpression of PITPalpha, but not PITPbeta or a PITPalpha mutant deficient in binding PtdIns, enhances laminin-dependent extension of axonal processes in hippocampal neurons, whereas knockdown of PITPalpha protein by siRNA suppresses laminin and BDNF-induced axonal growth.
The anti-apoptotic MAP kinase pathway is inhibited in NIH3T3 fibroblasts with increased expression of phosphatidylinositol transfer protein beta.
Snoek et al., Utrecht, Netherlands. In Biochim Biophys Acta, 2007
Mouse NIH3T3 fibroblast cells overexpressing phosphatidylinositol transfer protein beta (PI-TPbeta, SPIbeta cells) demonstrate a low rate of proliferation and a high sensitivity towards UV-induced apoptosis when compared with wtNIH3T3 cells.
[Comparison of urinary proteomics between steroid-sensitive and steroid-resistant minimal change nephrotic syndrome in children].
Chen et al., Nanjing, China. In Nan Fang Yi Ke Da Xue Xue Bao, 2007
Further analysis of 14 protein spots identified 12 proteins expressing in SRINS, namely kinesin family member 27, PITPNB, bullous pemphigoid antigen, alpha-1 protease inhibitor, Zn-alpha-2GP, alpha-1B-glycoprotein, serum albumin precursor, haptoglobin precursor, kinesin like motor protein, IRAK4, cytoplasmic dynein and cytokeratin 9. Nine of these 12 proteins were up-regulated (U1-U3, U5, U7-U9, U11-U12) and 3 down-regulated (D4, D6, D10) in SRINS, suggesting that these proteins may serve as the potential therapeutic targets and as new diagnostic markers for steroid-resistant nephrotic syndrome.
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.
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.
Differential expression of a C-terminal splice variant of phosphatidylinositol transfer protein beta lacking the constitutive-phosphorylated Ser262 that localizes to the Golgi compartment.
Cockcroft et al., London, United Kingdom. In Biochem J, 2006
in rat liver, the single gene for PITPbeta gives rise to seven distinct protein species that can be resolved on the basis of their charge differences
Specific and nonspecific membrane-binding determinants cooperate in targeting phosphatidylinositol transfer protein beta-isoform to the mammalian trans-Golgi network.
Bankaitis et al., Chapel Hill, United States. In Mol Biol Cell, 2006
PITPbeta localizes predominantly to the trans-Golgi network (TGN) and that this localization is independent of the phospholipid-bound state of PITPbeta.
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.
Phosphatidylinositol transfer proteins: emerging roles in cell proliferation, cell death and survival.
Snoek, Utrecht, Netherlands. In Iubmb Life, 2004
The actual cellular functions of the highly homologous small isoforms of the phosphatidylinositol transfer proteins, PI-TPalpha and PI-TPbeta have been studied using many different experimental conditions varying from in vitro experiments with purified proteins and lipid vesicles to investigations in animals.
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