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anti-Human PDCD6IP Antibodies:
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Human Polyclonal PDCD6IP Primary Antibody for WB - ABIN1881644
Inuzuka, Suzuki, Kawasaki, Shibata, Wakatsuki, Maki: Molecular basis for defect in Alix-binding by alternatively spliced isoform of ALG-2 (ALG-2DeltaGF122) and structural roles of F122 in target recognition. in BMC structural biology 2010
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Human Monoclonal PDCD6IP Primary Antibody for IF, IHC (p) - ABIN2477348
Bechmann, Weiss: Regulation of the proton/electron stoichiometry of mitochondrial ubiquinol:cytochrome c reductase by the membrane potential. in European journal of biochemistry / FEBS 1991
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Human Polyclonal PDCD6IP Primary Antibody for IF, IHC - ABIN347079
Mahul-Mellier, Hemming, Blot, Fraboulet, Sadoul: Alix, making a link between apoptosis-linked gene-2, the endosomal sorting complexes required for transport, and neuronal death in vivo. in The Journal of neuroscience : the official journal of the Society for Neuroscience 2006
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Human Polyclonal PDCD6IP Primary Antibody for IF, WB - ABIN523392
Kowal, Arras, Colombo, Jouve, Morath, Primdal-Bengtson, Dingli, Loew, Tkach, Théry: Proteomic comparison defines novel markers to characterize heterogeneous populations of extracellular vesicle subtypes. in Proceedings of the National Academy of Sciences of the United States of America 2016
Human Monoclonal PDCD6IP Primary Antibody for ICC, IF - ABIN260230
Haga, Yan, Takahashi, Matsuda, Patel: Extracellular Vesicles from Bone Marrow-Derived Mesenchymal Stem Cells Improve Survival from Lethal Hepatic Failure in Mice. in Stem cells translational medicine 2017
our results identify the CD63 (show CD63 Antibodies)-syntenin-1 (show SDCBP Antibodies)-ALIX complex as a key regulatory component in post-endocytic HPV trafficking.
Alix acts in concert with endophilin A to promote clathrin-independent endocytosis of cholera toxin and to regulate cell migration.
Revealed the transition of diffuse ALIX protein signals into a multivesicular body-like pattern during adenoma-carcinoma sequence in colorectal neoplasms.
Alix plays an important role in the proliferation of glioma cells and overexpression in gliomas predicts poor survival.
ALIX regulates P2Y1 (show P2RY1 Antibodies) degradation.
farnesylation of K-Ras (show HRAS Antibodies) was required for its packaging within extracellular nanovesicles, yet expressing a K-Ras (show HRAS Antibodies) farnesylation mutant did not decrease the number of nanovesicles or the amount of Alix protein released per cell.
These findings indicate that Alix binds to Ago2 (show EIF2C2 Antibodies) and miRNAs, suggesting that it plays a key role in miRNA enrichment during extracellular vesicles biogenesis.
The authors find that HIV-1 nucleocapsid mimics the PDZ (show INADL Antibodies) domains of syntenin (show SDCBP Antibodies), a membrane-binding adaptor involved in cell-to-cell contact/communication, to capture the Bro1 (show HMGCR Antibodies) domain of ALIX, which is an ESCRTs recruiting cellular adaptor.
We found that ARRDC3 is required for ALIX ubiquitination induced by activation of PAR1 (show MARK2 Antibodies)
phosphorylation of the intramolecular interaction site in the PRD (show PRD Antibodies) is one of the major mechanisms that activates the ESCRT function of ALIX
By interacting with F-actin, the Par (show AFG3L2 Antibodies) complex and ZO-1 (show TJP1 Antibodies), Alix ensures the formation and maintenance of the apically restricted actomyosin-tight junction complex.
ATG12 (show ATG12 Antibodies)-ATG3 (show ATG3 Antibodies) interacts with Alix to promote basal autophagic flux and late endosome function.
We have provided evidence that a promigratory function of galectin-3 (show LGALS3 Antibodies) may be mediated through interaction with its binding partner Alix.
Identify key role for syndecan (show SDC1 Antibodies)-syntenin (show SDCBP Antibodies)-ALIX in membrane transport and signalling processes.
the Ozz-E3 ligase regulates Alix at sites where the actin cytoskeleton undergoes remodeling.
Alix is a crucial mediator of Ca(2 (show CA2 Antibodies)+) induced caspase 9 (show CASP9 Antibodies) activation.
Biochemical characterization of two analogues of the apoptosis-linked gene 2 protein (show PDCD6 Antibodies) in Dictyostelium discoideum and interaction with murine Alix.
overexpression of Alix-CT leads to cytoplasmic vacuolization into tubulo-vesicular structures
We conclude that ALIX and ESCRT-III coordinately control abscission in Drosophila fGSCs and that their complex formation is required for accurate abscission timing in GSCs in vivo.
These findings establish that Xp95/Alix is phosphorylated within the proline-rich domain during M-phase induction, and indicate that the phosphorylation may both positively and negatively modulate their interaction with partner proteins.
This gene encodes a protein that functions within the ESCRT pathway in the abscission stage of cytokinesis, in intralumenal endosomal vesicle formation, and in enveloped virus budding. Studies using mouse cells have shown that overexpression of this protein can block apoptosis. In addition, the product of this gene binds to the product of the PDCD6 gene, a protein required for apoptosis, in a calcium-dependent manner. This gene product also binds to endophilins, proteins that regulate membrane shape during endocytosis. Overexpression of this gene product and endophilins results in cytoplasmic vacuolization, which may be partly responsible for the protection against cell death. Several alternatively spliced transcript variants encoding different isoforms have been found for this gene. Related pseudogenes have been identified on chromosome 15.
ALG-2 interacting protein 1
, ALG-2-interacting protein X
, PDCD6-interacting protein
, apoptosis-linked gene 2-interacting protein X
, dopamine receptor interacting protein 4
, programmed cell death 6-interacting protein
, ALG-2-interacting protein 1
, Alg2-interacting protein 1
, Alg2-interacting protein X
, E2f1-inducible protein
, ALG-2 interacting protein X
, programmed cell death 6 interacting protein
, Programmed cell death 6 interacting protein
, putative signal tranduction protein Xp95
, signal transduction protein Xp95