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GULP, engulfment adaptor PTB domain containing 1

The protein encoded by this gene is an adapter protein necessary for the engulfment of apoptotic cells by phagocytes. Several transcript variants, some protein coding and some thought not to be protein coding, have been found for this gene. [provided by RefSeq, Nov 2011] (from NCBI)
Top mentioned proteins: DOCK180, PTB, ELMO1, CAN, V1a
Papers on CED-6
Whole exome sequencing in a case of sporadic multiple meningioma reveals shared NF2, FAM109B, and TPRXL mutations, together with unique SMARCB1 alterations in a subset of tumor nodules.
Rey et al., Madrid, Spain. In Cancer Genet, Jun 2015
Mutations in other genes, such as IRS4, GULP1, NHSL1, and C10orf53, accounted for one alteration in each meningioma nodule.
EFF-1-mediated regenerative axonal fusion requires components of the apoptotic pathway.
Hilliard et al., Brisbane, Australia. In Nature, Feb 2015
PSR-1 functions cell-autonomously in the regrowing neuron and, instead of acting in its canonical signalling pathway, acts in a parallel phagocytic pathway that includes the transthyretin protein TTR-52, as well as CED-7, NRF-5 and CED-6 (refs 9, 10, 11, 12).
The adaptor protein GULP promotes Jedi-1-mediated phagocytosis through a clathrin-dependent mechanism.
Carter et al., Nashville, United States. In Mol Biol Cell, 2014
Here we demonstrate that Jedi-1 associates with GULP, the mammalian homologue of CED-6, an adaptor protein required for phagocytosis mediated by the nematode engulfment receptor CED-1.
Phagocytic receptor signaling regulates clathrin and epsin-mediated cytoskeletal remodeling during apoptotic cell engulfment in C. elegans.
Zhou et al., Houston, United States. In Development, 2013
Epistasis analysis places epn-1 and chc-1 in the same cell-corpse engulfment pathway as ced-1, ced-6 and dyn-1.
Clathrin and AP2 are required for phagocytic receptor-mediated apoptotic cell clearance in Caenorhabditis elegans.
Yang et al., Beijing, China. In Plos Genet, 2013
Importantly, we found that the phagocytic receptor CED-1 interacts with the α subunit of AP2, while the CED-6/Gulp adaptor forms a complex with both CHC-1 and the AP2 complex, which likely mediates the rearrangement of the actin cytoskeleton required for cell corpse engulfment triggered by the CED-1 signaling pathway.
Superparamagnetic iron oxide nanoparticles alter expression of obesity and T2D-associated risk genes in human adipocytes.
Rezaee et al., Groningen, Netherlands. In Sci Rep, 2012
mRNA of GULP1, SLC30A8, NEGR1, SEC16B, MTCH2, MAF, MC4R, and TMEM195 were severely induced, whereas INSIG2, NAMPT, MTMR9, PFKP, KCTD15, LPL and GNPDA2 were down-regulated upon SPIONs stimulation.
Engulfment protein GULP is regulator of transforming growth factor-β response in ovarian cells.
Kiss et al., Montréal, Canada. In J Biol Chem, 2012
GULP expression positively regulates TGF-beta signaling leading to growth inhibition, this may represent an attractive target to achieve TGF-beta responsiveness in ovarian cells.
The apoptotic engulfment protein Ced-6 participates in clathrin-mediated yolk uptake in Drosophila egg chambers.
Traub et al., Pittsburgh, United States. In Mol Biol Cell, 2012
The apoptotic engulfment protein Ced-6 participates in clathrin-mediated yolk uptake in Drosophila egg chambers.
Engulfment adapter PTB domain containing 1 interacts with and affects processing of the amyloid-β precursor protein.
von Arnim et al., Ulm, Germany. In Neurobiol Aging, 2012
This study identify GULP1 as a novel neuronal amyloid-beta precursor protein interacting protein that alters trafficking and processing of amyloid-beta precursor protein.
GULP1 is a novel APP-interacting protein that alters APP processing.
Lau et al., Hong Kong, Hong Kong. In Biochem J, 2011
overexpression of GULP1 enhanced the generation of APP CTFs (C-terminal fragments) and Abeta, whereas knockdown of GULP1 suppressed APP CTFs and Abeta production.
Adaptor protein GULP is involved in stabilin-1-mediated phagocytosis.
Kim et al., Kyŏngju, South Korea. In Biochem Biophys Res Commun, 2010
these results indicate that GULP functions as an adaptor protein for stabilin-1-mediated phagocytosis.
Caenorhabditis elegans transthyretin-like protein TTR-52 mediates recognition of apoptotic cells by the CED-1 phagocyte receptor.
Xue et al., Boulder, United States. In Nat Cell Biol, 2010
Genetic analysis indicates that TTR-52 acts in the cell corpse engulfment pathway mediated by CED-1, CED-6 and CED-7 and affects clustering of the phagocyte receptor CED-1 around apoptotic cells.
Journey to the grave: signaling events regulating removal of apoptotic cells.
Ravichandran et al., Charlottesville, United States. In J Cell Sci, 2007
Two potential signaling modules have been identified: one involving the CED-12/ELMO and CED-5/Dock180 proteins, which function as a bipartite guanine nucleotide exchange factor (GEF) for Rac1, and a second involving CED-1/LRP1 (a potential engulfment receptor) and the adaptor protein CED-6/GULP.
Two pathways converge at CED-10 to mediate actin rearrangement and corpse removal in C. elegans.
Hengartner et al., Stony Brook, United States. In Nature, 2005
In the second group, the candidate receptor CED-1 (CD91/LRP/SREC) probably recognizes an unknown ligand on the apoptotic cell and signals via its cytoplasmic tail to the adaptor protein CED-6 (hCED-6/GULP), whereas CED-7 (ABCA1) is thought to play a role in membrane dynamics.
Programmed cell death.
Xue et al., United States. In Wormbook, 2004
The recognition and removal of the dying cell is mediated by two partially redundant signaling pathways involving CED-1, CED-6 and CED-7 in one pathway and CED-2, CED-5, CED-10, CED-12 and PSR-1 in the other pathway.
The engulfment process of programmed cell death in caenorhabditis elegans.
Horvitz et al., Salt Lake City, United States. In Annu Rev Cell Dev Biol, 2003
Components of the cell-corpse recognition system of one of the C. elegans pathways include the CED-7 ABC transporter, which likely presents a death ligand on the surface of the dying cell; the CED-1 transmembrane receptor, which recognizes this signal; and the CED-6 adaptor protein, which may transduce a signal from CED-1.
Phagocytosis promotes programmed cell death in C. elegans.
Horvitz et al., Cambridge, United States. In Nature, 2001
In the nematode Caenorhabditis elegans programmed cell death requires the killer genes egl-1, ced-4 and ced-3 (refs 1 and 2), and the engulfment of dying cells requires the genes ced-1, ced-2, ced-5, ced-6, ced-7, ced-10 and ced-12 (refs 3,4,5).
The molecular mechanism of programmed cell death in C. elegans.
Hengartner et al., New York City, United States. In Ann N Y Acad Sci, 1998
These 15 genes have been divided into four groups based on the order of their activity during the process of programmed cell death: (1) those involved in the decision making (ces-1 and ces-2); (2) in the process of execution (ced-3, ced-4, ced-9 and egl-1); (3) in the engulfment of dying cells by engulfing cells (ced-1, ced-2, ced-5, ced-6, ced-7, ced-10, ced-12); and (4) those in the degradation of cell corpses within engulfing cells (nuc-1).
Candidate adaptor protein CED-6 promotes the engulfment of apoptotic cells in C. elegans.
Hengartner et al., New York City, United States. In Cell, 1998
Here we report the cloning and functional characterization of ced-6, a gene specifically required for the engulfment of apoptotic cells in the nematode C. elegans.
Cell death in C. elegans: molecular insights into mechanisms conserved between nematodes and mammals.
Driscoll, United States. In Brain Pathol, 1996
Once cells die, corpses are phagocytized and consumed in what appear to be at least two parallel pathways that require the activities of ced-1, ced-6, ced-7 and ced-2, ced-5, ced-10.
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