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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.
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.
DAB2IP (show DAB2IP Proteins) loss reprograms intracellular signal transduction and anti-apoptotic gene expression, which potentiates prostate cancer cell survival from androgen deprivation therapy-induced cell death.
Germ cell-specific or Sertoli cell-specific deletion of Aip1 gene each led to significant defects in germ cell migration after postnatal day 4 or 5, accompanied by elevated levels of actin filaments (F-actin) in the affected cells.
Cor1B, Cof1 and AIP1 work in concert through a temporally ordered pathway to induce highly efficient severing and disassembly of actin filaments.
results suggest that Dab2IP plays an important role in the migration and positioning of a subpopulation of later-born (layers II-IV) neurons, likely through the regulation of Rap1 and integrin signaling.
Our data reveal that AIP1, by inhibiting VEGFR2 (show KDR Proteins)-dependent signaling in tumor niche, suppresses tumor EMT (show ITK Proteins) switch, tumor angiogenesis, and tumor premetastatic niche formation to limit tumor growth and metastasis.
AIP1 was elevated in the brain of AD Tg2576 mice. Abeta1-42 treatment induced the interaction of AIP1 and ASK1 (show MAP3K5 Proteins), which led to dissociation of ASK1 (show MAP3K5 Proteins) and 14-3-3 (show YWHAQ Proteins).
site-specific methylation of mDab2ip gene during cerebellar development may play a role in inclusion of exon 5, resulting in a Dab2ip (show DAB2IP Proteins) transcript variant that encodes a full pleckstrin (show PLEK Proteins) homology (PH) domain.
ATG12 (show ATG12 Proteins)-ATG3 (show ATG3 Proteins) interacts with Alix to promote basal autophagic flux and late endosome function.
Study showed that DAB2IP (show DAB2IP Proteins) can be functionally inactivated by physical interaction with mutant p53 (show TP53 Proteins) proteins with implications for the response of cancer cells to inflammatory cytokines.
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.
MRTF-A-miR (show MLXIP Proteins)-206-WDR1 (show WDR1 Proteins) form feedback loop to regulate breast cancer cell migration.
Alix plays an important role in the proliferation of glioma cells and overexpression in gliomas predicts poor survival.
homozygous missense L153F/L293F mutation in the actin regulatory gene WDR1 (show WDR1 Proteins) causes a new autoinflammatory disease in humans, with periodic fevers, immunodeficiency, and intermittent thrombocytopenia (PFIT).
These data suggest that WDR1 (show WDR1 Proteins) plays an important role in suppressing platelet activity, where it alters the actin cytoskeleton dynamics, and downregulation of WDR1 (show WDR1 Proteins) may contribute to the platelet-mediated pathogenesis of cardiovascular disease.
Mutations in WDR1 (show WDR1 Proteins) affect neutrophil morphology, motility, and function, causing a novel primary immunodeficiency
ALIX regulates P2Y1 (show P2RY1 Proteins) degradation.
Identify positive correlations between WDR1 (show WDR1 Proteins) and CLNK (show CLNK Proteins) gene polymorphisms in Chinese-Tibetan gout populations.
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.
This gene encodes a protein containing 9 WD repeats. WD repeats are approximately 30- to 40-amino acid domains containing several conserved residues, mostly including a trp-asp at the C-terminal end. WD domains are involved in protein-protein interactions. The encoded protein may help induce the disassembly of actin filaments. Two transcript variants encoding different isoforms have been found for this gene.
ALG-2 interacting protein 1
, programmed cell death 6-interacting protein
, programmed cell death 6 interacting protein
, Programmed cell death 6 interacting protein
, ASK-interacting protein 1
, ASK1-interacting protein 1
, DAB2-interacting protein
, DOC-2/DAB-2 interactive protein
, disabled 2 interacting protein long form
, disabled homolog 2 interacting protein
, disabled homolog 2-interacting protein
, putative signal tranduction protein Xp95
, signal transduction protein Xp95
, ALG-2-interacting protein X
, PDCD6-interacting protein
, apoptosis-linked gene 2-interacting protein X
, dopamine receptor interacting protein 4
, ALG-2-interacting protein 1
, Alg2-interacting protein 1
, Alg2-interacting protein X
, E2f1-inducible protein
, ALG-2 interacting protein X
, WD repeat-containing protein 1
, actin-interacting protein 1