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Programmed cell death 6 interacting protein

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. [provided by RefSeq, Jan 2012] (from NCBI)
Top mentioned proteins: Actin, cofilin, CAN, ALG-2, ACID
Papers on AIP1
Actin-interacting Protein 1 Promotes Disassembly of Actin-depolymerizing Factor/Cofilin-bound Actin Filaments in a pH-dependent Manner.
Ono et al., United States. In J Biol Chem, Feb 2016
UNASSIGNED: Actin-interacting protein 1 (AIP1) is a conserved WD-repeat protein that promotes disassembly of actin filaments when actin-depolymerizing factor (ADF)/cofilin is present.
Analysis of assembly and budding of Lujo virus.
Yasuda et al., South Africa. In J Virol, Jan 2016
The L-domains in Z are required for efficient virus-like particle release, but Tsg101, ALIX/AIP1, and Vps4A/B are unnecessary for budding.
A Novel Monoclonal Antibody Against Human DAB2IP.
Hu et al., Chengdu, China. In Monoclon Antib Immunodiagn Immunother, Aug 2015
DAB2 interactive protein (DAB2IP), also known as ASK1-interacting protein-1 (AIP1), a novel member of the RasGTPase-activating protein family, plays a key role in tumor suppression during cancer progression and is highly expressed in vascular smooth muscle cells (VSMCs) and endothelial cells (ECs).
AIP1-mediated stress signaling in atherosclerosis and arteriosclerosis.
Min et al., Guangzhou, China. In Curr Atheroscler Rep, May 2015
AIP1 (ASK1-interacting protein-1; encoded by the DAB2IP gene), a signaling scaffolding protein, is abundantly expressed in vascular endothelial cells (EC).
AIP1-mediated actin disassembly is required for postnatal germ cell migration and spermatogonial stem cell niche establishment.
Chen et al., Nanjing, China. In Cell Death Dis, 2014
Here, we show that the actin disassembly factor actin interacting protein 1 (AIP1) is required in both germ cells and Sertoli cells to regulate this process.
Identification of novel HIV-1 dependency factors in primary CCR4(+)CCR6(+)Th17 cells via a genome-wide transcriptional approach.
Ancuta et al., Montréal, Canada. In Retrovirology, 2014
A meta-analysis using the NCBI HIV Interaction Database revealed a set of Th17-specific HIV dependency factors (HDFs): PARG, PAK2, KLF2, ITGB7, PTEN, ATG16L1, Alix/AIP1/PDCD6IP, LGALS3, JAK1, TRIM8, MALT1, FOXO3, ARNTL/BMAL1, ABCB1/MDR1, TNFSF13B/BAFF, and CDKN1B.
AIP1 is a novel Agenet/Tudor domain protein from Arabidopsis that interacts with regulators of DNA replication, transcription and chromatin remodeling.
Hemerly et al., Rio de Janeiro, Brazil. In Bmc Plant Biol, 2014
Furthermore, we characterized a member from Arabidopsis thaliana named AIP1 that harbors Agenet/Tudor and DUF724 domains.
AIP1 acts with cofilin to control actin dynamics during epithelial morphogenesis.
Chen et al., Nanjing, China. In Development, 2012
AIP1 enhances cofilin-mediated actin disassembly in the apical region of precluster cells to promote remodeling of adherense junctions.
BRCA2 localization to the midbody by filamin A regulates cep55 signaling and completion of cytokinesis.
Couch et al., Rochester, United States. In Dev Cell, 2012
At the midbody, BRCA2 influences the recruitment of endosomal sorting complex required for transport (ESCRT)-associated proteins, Alix and Tsg101, and formation of CEP55-Alix and CEP55-Tsg101 complexes during abscission.
Syndecan-syntenin-ALIX regulates the biogenesis of exosomes.
David et al., Leuven, Belgium. In Nat Cell Biol, 2012
Identify key role for syndecan-syntenin-ALIX in membrane transport and signalling processes.
Structural recognition mechanisms between human Src homology domain 3 (SH3) and ALG-2-interacting protein X (Alix).
Morelli et al., Marseille, France. In Febs Lett, 2012
Structural recognition mechanisms between human Src homology domain 3 (SH3) and ALG-2-interacting protein X (Alix
Zebrafish arl6ip1 is required for neural crest development during embryogenesis.
Tsai et al., Taipei, Taiwan. In Plos One, 2011
arl6ip1 is required for neural crest migration and sublineage specification.
AIP1 in graft arteriosclerosis.
Pober et al., New Haven, United States. In Trends Cardiovasc Med, 2011
We have exploited the power of mouse genetics to examine the function of AIP1, a signaling adaptor molecule involved in vascular inflammation, in two newly established IFN-γ-mediated models of GA.
[Envelope virus assembly and budding].
Irie, Hiroshima, Japan. In Uirusu, 2010
Among such viruses, we have been focusing on Sendai virus (SeV) and shown that (i) SeV M functionally and physically interact with a component of the ESCRT complex, Alix/AIP1, although budding of M-VLPs does not seem to be dependent on the pathway; (ii) one of the accessory proteins of SeV, C, also interact with Alix/AIP1, and recruit it to the plasma membrane for efficient budding of M-VLPs; (iii) the C protein regulate balance of viral genome and antigenome RNA synthesis for optimized production of infectious virus particles.
Inside view of cell locomotion through single-molecule: fast F-/G-actin cycle and G-actin regulation of polymer restoration.
Watanabe, Kyoto, Japan. In Proc Jpn Acad Ser B Phys Biol Sci, 2009
This fast F-actin turnover is facilitated by the filament severing/disrupting activity involving cofilin and AIP1.
Molecular assemblies and membrane domains in multivesicular endosome dynamics.
Gruenberg et al., Genève, Switzerland. In Exp Cell Res, 2009
This process depends on the late endosomal lipid lysobisphosphatidic acid and its putative effector Alix/AIP1, and is presumably coupled to the invagination of the endosomal limiting membrane at the molecular level via ESCRT proteins.
Structural and biochemical studies of ALIX/AIP1 and its role in retrovirus budding.
Hill et al., Salt Lake City, United States. In Cell, 2007
Crystal structure; ALIX serves as a flexible, extended scaffold that connects retroviral Gag proteins to ESCRT-III and other cellular-budding machinery
Endosome-to-cytosol transport of viral nucleocapsids.
Gruenberg et al., Genève, Switzerland. In Nat Cell Biol, 2005
This last step, which initiates infection, depends on the late endosomal lipid lysobisphosphatidic acid (LBPA) and its putative effector Alix/AIP1, and is regulated by phosphatidylinositol-3-phosphate (PtdIns3P) signalling via the PtdIns3P-binding protein Snx16.
The protein network of HIV budding.
Sundquist et al., Salt Lake City, United States. In Cell, 2003
These proteins were connected into a coherent network by 43 different protein-protein interactions, with AIP1 playing a key role in linking complexes that act early (TSG101/ESCRT-I) and late (CHMP4/ESCRT-III) in the pathway.
AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding.
Göttlinger et al., Boston, United States. In Cell, 2003
We now show that HIV Gag p6 contains a second region involved in L domain function that binds AIP1, a homolog of the yeast class E Vps protein Bro1.
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