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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 Proteins) degradation.
farnesylation of K-Ras (show HRAS Proteins) was required for its packaging within extracellular nanovesicles, yet expressing a K-Ras (show HRAS Proteins) 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 Proteins) 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 domains of syntenin (show SDCBP Proteins), a membrane-binding adaptor involved in cell-to-cell contact/communication, to capture the Bro1 (show HMGCR Proteins) 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 Proteins)
phosphorylation of the intramolecular interaction site in the PRD is one of the major mechanisms that activates the ESCRT function of ALIX
homologous domain of human Bro1 (show HMGCR Proteins) domain-containing proteins, Alix and Brox, binds CHMP4B (show CHMP4A Proteins) but not STAM2 (show STAM2 Proteins), despite their high structural similarity
ATG12 (show ATG12 Proteins)-ATG3 (show ATG3 Proteins) 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 Proteins) may be mediated through interaction with its binding partner Alix.
Identify key role for syndecan (show SDC1 Proteins)-syntenin (show SDCBP Proteins)-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 Proteins)+) induced caspase 9 (show CASP9 Proteins) activation.
Biochemical characterization of two analogues of the apoptosis-linked gene 2 protein (show PDCD6 Proteins) in Dictyostelium discoideum and interaction with murine Alix.
overexpression of Alix-CT leads to cytoplasmic vacuolization into tubulo-vesicular structures
interaction of Gag with Tsg101 and Alix favors budding from the plasma membrane and relieves a requirement for ubiquitination by Nedd4
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