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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

SNF7 Snf7p

Snf7, Snf7p, CHMP4b, CHMP4, Vps32, CHMP4a, hSnf7-1
CHMP4A belongs to the chromatin-modifying protein/charged multivesicular body protein (CHMP) family. These proteins are components of ESCRT-III (endosomal sorting complex required for transport III), a complex involved in degradation of surface receptor proteins and formation of endocytic multivesicular bodies (MVBs). Some CHMPs have both nuclear and cytoplasmic/vesicular distributions, and one such CHMP, CHMP1A (MIM 164010), is required for both MVB formation and regulation of cell cycle progression (Tsang et al., 2006 [PubMed 16730941]).[supplied by OMIM, Mar 2008] (from NCBI)
Top mentioned proteins: Vps4, TSG101, CAN, Vps24, ATPase
Papers on Snf7
Cell layer-specific distribution of transiently expressed barley ESCRT-III component HvVPS60 in developing barley endosperm.
New
Ibl et al., Vienna, Austria. In Protoplasma, Jan 2016
We used fluorescently tagged core ESCRT-III members HvSNF7a/CHMP4 and HvVPS24/CHMP3 and the associated ESCRT-III component HvVPS60a/CHMP5 for transient localization studies in barley endosperm.
Negative membrane curvature catalyzes nucleation of endosomal sorting complex required for transport (ESCRT)-III assembly.
New
Hurley et al., Berkeley, United States. In Proc Natl Acad Sci U S A, Jan 2016
The assembly of the core ESCRT-III subunit CHMP4B/Snf7 is preferentially nucleated in the resulting 100-nm-deep membrane concavities.
The α-arrestin ARRDC3 mediates ALIX ubiquitination and G protein-coupled receptor lysosomal sorting.
New
Trejo et al., San Diego, United States. In Mol Biol Cell, Jan 2016
Depletion of ARRDC3 by small interfering RNA disrupts ALIX interaction with activated PAR1 and the CHMP4B ESCRT-III subunit, suggesting that ARRDC3 regulates ALIX activity.
The Mammalian Orthologs of Drosophila Lgd, CC2D1A and CC2D1B, Function in the Endocytic Pathway, but Their Individual Loss of Function Does Not Affect Notch Signalling.
New
Klein et al., Düsseldorf, Germany. In Plos Genet, Dec 2015
Moreover, the Drosophila melanogaster ortholog Lgd was shown to be involved in the endosomal trafficking of the Notch receptor and other transmembrane receptors and physically interacts with the ESCRT-III component Shrub/CHMP4.
ESCRT proteins restrict constitutive NF-κB signaling by trafficking cytokine receptors.
New
Miaczynska et al., Warsaw, Poland. In Sci Signal, Dec 2015
We depleted all of the ESCRT (endosomal sorting complexes required for transport) subunits, which mediate receptor trafficking and degradation, and found that the components Tsg101, Vps28, UBAP1, and CHMP4B were essential to restrict constitutive NF-κB signaling in human embryonic kidney 293 cells.
ESCRT (Endosomal Sorting Complex Required for Transport) Machinery Is Essential for Acrosomal Exocytosis in Human Sperm.
New
Mayorga et al., Mendoza, Argentina. In Biol Reprod, Nov 2015
We report here that members of ESCRT I (TSG101), ESCRT III (CHMP4), and the AAA ATPase VPS4 are present in the acrosomal region of the human sperm.
Chitosan, Carbon Quantum Dot, and Silica Nanoparticle Mediated dsRNA Delivery for Gene Silencing in Aedes aegypti: A Comparative Analysis.
New
Palli et al., Lexington, United States. In Acs Appl Mater Interfaces, Oct 2015
We tested three nanoparticles, chitosan, carbon quantum dot (CQD), and silica complexed with dsRNA, to target two mosquito genes (SNF7 and SRC) for controlling Aedes aegypti larvae.
ESCRT-III-Associated Protein ALIX Mediates High-Affinity Phosphate Transporter Trafficking to Maintain Phosphate Homeostasis in Arabidopsis.
New
Rubio et al., Madrid, Spain. In Plant Cell, Sep 2015
Here, we describe ALIX, a cytosolic protein that associates with MVB by interacting with ESCRT-III subunit SNF7 and mediates PHT1;1 trafficking to the vacuole in Arabidopsis thaliana.
ESCRT-III controls nuclear envelope reformation.
New
Impact
Carlton et al., Bristol, United Kingdom. In Nature, Jul 2015
The ESCRT-III component charged multivesicular body protein 2A (CHMP2A) is directed to the forming NE through binding to CHMP4B, and provides an activity essential for NE reformation.
High CHMP4B expression is associated with accelerated cell proliferation and resistance to doxorubicin in hepatocellular carcinoma.
New
Wan et al., Nantong, China. In Tumour Biol, Apr 2015
Charged multivesicular body protein 4B (CHMP4B), a subunit of the endosomal sorting complex required for transport (ESCRT)-III complex, plays an important part in cytokinetic membrane abscission and the late stage of mitotic cell division.
Distribution of ESCRT machinery at HIV assembly sites reveals virus scaffolding of ESCRT subunits.
Impact
Lippincott-Schwartz et al., Bethesda, United States. In Science, 2014
We observed ESCRT subunits localized within the head of budding virions and released particles, with head-localized levels of CHMP2A decreasing relative to Tsg101 and CHMP4B upon virus abscission.
CC2D1A is a regulator of ESCRT-III CHMP4B.
GeneRIF
Weissenhorn et al., Grenoble, France. In J Mol Biol, 2012
CHMP4B interacts directly with CC2D1A and CC2D1B with nanomolar affinity by forming a 1:1 complex.
Regulation of CHMP4/ESCRT-III function in human immunodeficiency virus type 1 budding by CC2D1A.
GeneRIF
Göttlinger et al., Worcester, United States. In J Virol, 2012
CC2D1A interaction with CHMP4B/4A blocks HIV-1 budding.
ESCRT-III subunits Snf7-1 and Snf7-2 differentially regulate transmembrane cargos in hESC-derived human neurons.
GeneRIF
Gao et al., Taejŏn, South Korea. In Mol Brain, 2010
hSnf7-1 and hSnf7-2 are preferentially associated with CHMP2A and CHMP2B, respectively, and regulate the turnover of distinct transmembrane cargos such as neurotransmitter receptors in human neurons.
High-throughput screening identifies CHMP4A associated with hypoxia-inducible factor 1.
GeneRIF
Ma et al., Beijing, China. In Life Sci, 2010
our results show that CHMP4A significantly enhances the stability and transcriptional activity of HIF-1alpha both under normoxic and hypoxic conditions
PtdIns(3)P controls cytokinesis through KIF13A-mediated recruitment of FYVE-CENT to the midbody.
Impact
Stenmark et al., Oslo, Norway. In Nat Cell Biol, 2010
We show that PtdIns(3)P localizes to the midbody during cytokinesis and recruits a centrosomal protein, FYVE-CENT (ZFYVE26), and its binding partner TTC19, which in turn interacts with CHMP4B, an endosomal sorting complex required for transport (ESCRT)-III subunit implicated in the abscission step of cytokinesis.
[Progress in pathogenic genes and their functions of congenital cataract].
Review
Cheng et al., Beijing, China. In Zhonghua Yan Ke Za Zhi, 2010
Currently, at least 22 specific genes associated with isolated inherited cataract have been identified: ten crystallin genes: CRYAA, CRYAB, CRYBA1/A3, CRYBA4, CRYBB1, CRYBB2, CRYBB3, CRYGC, CRYGD, CRYGS; 4 membrane protein genes: GJA3, GJA8, MIP, LIM2; three growth and transcription factor genes: PITX3, MAF, HSF4; two cytoskeletal protein gene: BSFP1, BSFP2; chromatin modifying protein-4B gene: CHMP4B, EPHA2 and NHS, it is likely that more genes remain to be discovered.
Analysis of the dual function of the ESCRT-III protein Snf7 in endocytic trafficking and in gene expression.
GeneRIF
Kölling et al., Stuttgart, Germany. In Biochem J, 2009
By generating SNF7 mutations that severely affect endocytic trafficking, but leave the Rim pathway function intact, data show that the two functions of SNF7 can be separated genetically.
Structural and biochemical studies of ALIX/AIP1 and its role in retrovirus budding.
Impact
Hill et al., Salt Lake City, United States. In Cell, 2007
YPX(n)L late domains bind in a conserved hydrophobic pocket on the second arm near the apex of the V, whereas CHMP4/ESCRT-III proteins bind a conserved hydrophobic patch on the Bro1 domain, and both interactions are required for virus budding.
The protein network of HIV budding.
Impact
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.
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