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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Pleckstrin homology domain containing, family A

Top mentioned proteins: V1a, GLTP, STEP, p16, CIs
Papers on FAPP2
Specificity of the mammalian glycolipid transfer proteins.
Mattjus, Turku, Finland. In Chem Phys Lipids, Jan 2016
Currently the unique GLTP-fold specific for binding glycosphingolipids is found only in the founding member GLTP and the phosphoinositol 4-phosphate adapter protein 2, FAPP2.
Sphingolipid metabolism and interorganellar transport: localization of sphingolipid enzymes and lipid transfer proteins.
Hanada et al., Tokyo, Japan. In Traffic, Feb 2015
These LTPs consist of ceramide transfer protein (CERT), four-phosphate adaptor protein 2 (FAPP2) and ceramide-1-phosphate transfer protein (CPTP), respectively.
Modulation of hepatitis C virus genome replication by glycosphingolipids and four-phosphate adaptor protein 2.
Konan et al., Albany, United States. In J Virol, 2014
To test this hypothesis, we generated cell lines for doxycycline-inducible expression of short hairpin RNAs (shRNAs) targeting the PI4P effector, four-phosphate adaptor protein 2 (FAPP2).
Membranes and mammalian glycolipid transferring proteins.
Mattjus et al., Turku, Finland. In Chem Phys Lipids, 2014
Here we review the latest advances in the glycolipid transfer protein (GLTP) and the phosphoinositol 4-phosphate adaptor protein-2 (FAPP2) field, from a membrane point of view.
Vesicular and non-vesicular transport feed distinct glycosylation pathways in the Golgi.
De Matteis et al., Napoli, Italy. In Nature, 2013
We previously identified a non-vesicular intra-Golgi transport pathway for glucosylceramide (GlcCer)--the common precursor of the different series of glycosphingolipids-that is operated by the cytosolic GlcCer-transfer protein FAPP2 (also known as PLEKHA8) (ref.
The glycolipid transfer protein (GLTP) domain of phosphoinositol 4-phosphate adaptor protein-2 (FAPP2): structure drives preference for simple neutral glycosphingolipids.
Brown et al., Austin, United States. In Biochim Biophys Acta, 2013
Phosphoinositol 4-phosphate adaptor protein-2 (FAPP2) plays a key role in glycosphingolipid (GSL) production using its C-terminal domain to transport newly synthesized glucosylceramide away from the cytosol-facing glucosylceramide synthase in the cis-Golgi for further anabolic processing.
Connecting vesicular transport with lipid synthesis: FAPP2.
De Matteis et al., Napoli, Italy. In Biochim Biophys Acta, 2012
FAPP2 functions in both membrane trafficking and lipid metabolism in a fashion that integrates its activities in membrane trafficking and in lipid transfer. (Review)
Reconstitution of glucosylceramide flip-flop across endoplasmic reticulum: implications for mechanism of glycosphingolipid biosynthesis.
Menon et al., New York City, United States. In J Biol Chem, 2012
179, 101-115) proposed that this essential flipping step is accomplished via a complex trafficking itinerary; GlcCer is moved from the cytoplasmic face of the Golgi to the endoplasmic reticulum (ER) by FAPP2, a cytoplasmic lipid transfer protein, flipped across the ER membrane, then delivered to the lumen of the Golgi complex by vesicular transport.
A 14-3-3γ dimer-based scaffold bridges CtBP1-S/BARS to PI(4)KIIIβ to regulate post-Golgi carrier formation.
Corda et al., Napoli, Italy. In Nat Cell Biol, 2012
Several components of the underlying molecular machinery have been identified, including those involved in the budding/initiation of tubular carrier precursors (for example, the phosphoinositide kinase PI(4)KIIIβ, the GTPase ARF, and FAPP2), and in the fission of these precursors (for example, PKD, CtBP1-S/BARS).
Analysis of the key elements of FFAT-like motifs identifies new proteins that potentially bind VAP on the ER, including two AKAPs and FAPP2.
Levine et al., London, United Kingdom. In Plos One, 2011
By defining FFAT-like motifs more widely than before, we found them in novel proteins the functions of which had not previously been directly linked to the ER, including: two PKA anchoring proteins, AKAP220 and AKAP110; a family of plant LTPs; and the glycolipid LTP phosphatidylinositol-four-phosphate adaptor-protein-2 (FAPP-2).
Human glycolipid transfer protein (GLTP) expression modulates cell shape.
Brown et al., Austin, United States. In Plos One, 2010
Glycolipid transfer protein (GLTP) accelerates glycosphingolipid (GSL) intermembrane transfer via a unique lipid transfer/binding fold (GLTP-fold) that defines the GLTP superfamily and is the prototype for GLTP-like domains in larger proteins, i.e. phosphoinositol 4-phosphate adaptor protein-2 (FAPP2).
Golgi protein FAPP2 tubulates membranes.
Simons et al., Dresden, Germany. In Proc Natl Acad Sci U S A, 2010
Data show that FAPP2 is present in tubules forming from the trans-Golgi in epithelial MDCK cells.
FAPP2 gene downregulation increases tumor cell sensitivity to Fas-induced apoptosis.
Kruse et al., San Diego, United States. In Biochem Biophys Res Commun, 2009
These data demonstrate a previously unknown role for FAPP2 in conferring resistance to apoptosis and indicate that FAPP2 may be a target for cancer therapy.
Two sphingolipid transfer proteins, CERT and FAPP2: their roles in sphingolipid metabolism.
Hanada et al., Tokyo, Japan. In Iubmb Life, 2008
Recent discoveries of two sphingolipid transfer proteins, CERT and FAPP2, have brought the field of sphingolipid metabolism to a more dynamic stage.
Glycosphingolipid synthesis requires FAPP2 transfer of glucosylceramide.
De Matteis et al., Chieti, Italy. In Nature, 2007
by coupling the synthesis of glycosphingolipids with their export to the cell surface, FAPP2 emerges as crucial in determining the lipid identity and composition of the plasma membrane
FAPP2, cilium formation, and compartmentalization of the apical membrane in polarized Madin-Darby canine kidney (MDCK) cells.
Simons et al., Dresden, Germany. In Proc Natl Acad Sci U S A, 2007
Data demonstrate FAPP2 is required for cilium formation in polarized MDCK cells.
FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and PtdIns(4)P.
De Matteis et al., Santa Maria, Brazil. In Nat Cell Biol, 2004
Data show that FAPP1 and 2 are essential components of a phosphatidylinositol 4-phosphate- and ADP-ribosylation factor-regulated machinery that controls generation of constitutive post-Golgi carriers.
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