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VPS28 Vps28p

VPS28, Vps28p, hVPS28
This gene encodes a protein involved in endosomal sorting of cell surface receptors via a multivesicular body/late endosome pathway. The encoded protein is one of the three subunits of the ESCRT-I complex (endosomal complexes required for transport) involved in the sorting of ubiquitinated proteins. The two other subunits of ESCRT-I are vesicular protein sorting 23, also known as tumor susceptibility gene 101 (TSG101), and vesicular protein sorting 37. Two alternative transcripts encoding different isoforms have been described. Additional alternative transcripts may exist but the proteins encoded by these transcripts have not been verified experimentally. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: TSG101, V1a, Vps4, CAN, ATPase
Papers using VPS28 antibodies
Hrs regulates multivesicular body formation via ESCRT recruitment to endosomes
Supplier
Stenmark Harald et al., In The Journal of Cell Biology, 1999
... ) and hVps28 (Bishop and Woodman, 2001) were amplified by PCR from a marathon-ready HeLa cDNA (CLONTECH Laboratories, Inc.) and verified ...
Papers on VPS28
Identification of the endosomal sorting complex required for transport-I (ESCRT-I) as an important modulator of anti-miR uptake by cancer cells.
Wiederschain et al., Cambridge, United States. In Nucleic Acids Res, 2015
RNA interference-mediated knockdown of TSG101 and another ESCRT-I protein, VPS28, improved uptake of anti-miR-21 in parental SKHEP1 cells and restored productive uptake to SKHEP1 clones with acquired resistance to anti-miR-21.
Quantitative Proteomic Analysis of BHK-21 Cells Infected with Foot-and-Mouth Disease Virus Serotype Asia 1.
Liu et al., Lanzhou, China. In Plos One, 2014
Among these proteins, six cellular proteins, including three down-regulated (VPS28, PKR, EVI5) and three up-regulated (LYPLA1, SEC62 and DARs), were selected according to the significance of the changes and/or the relationship with PKR.
A genome-wide small interfering RNA (siRNA) screen reveals nuclear factor-κB (NF-κB)-independent regulators of NOD2-induced interleukin-8 (IL-8) secretion.
Núñez et al., Ann Arbor, United States. In J Biol Chem, 2014
Using immortalized macrophages, we validate the ubiquitin protease, USP8, and the endosomal sorting protein, VPS28, as negative regulators of NOD2-induced cytokine secretion.
CIIA negatively regulates the Ras-Erk1/2 signaling pathway through inhibiting the Ras-specific GEF activity of SOS1.
Choi et al., Seoul, South Korea. In J Cell Sci, 2014
In this study, we show that CIIA (also known as VPS28) physically associates with SOS1 and thereby inhibits the GEF activity of SOS1 on Ras, which prevents the epidermal growth factor (EGF)-induced activation of the Ras-Erk1/2 pathway.
The molecular basis for selective assembly of the UBAP1-containing endosome-specific ESCRT-I complex.
Woodman et al., Manchester, United Kingdom. In J Cell Sci, 2014
ESCRT-I has four subunits; TSG101, VPS28, VPS37 and MVB12.
A complex network of interactions between mitotic kinases, phosphatases and ESCRT proteins regulates septation and membrane trafficking in S. pombe.
McInerny et al., Glasgow, United Kingdom. In Plos One, 2013
Multiple observations indicate functional interplay between polo and ESCRT components: firstly, two-hybrid in vivo interactions are reported between Plo1p and Sst4p, Vps28p, Vps25p, Vps20p and Vps32p; secondly, co-immunoprecipitation of human homologues of Vps20p, Vps32p, Vps24p and Vps2p by human Plk1; and thirdly, in vitro phosphorylation of budding yeast Vps32p and Vps20p by polo kinase.
Involvement of ESCRT-II in hepatitis B virus morphogenesis.
Prange et al., Mainz, Germany. In Plos One, 2013
RNA interference knockdown of the ESCRT-I subunits TSG101 and VPS28 did not block, but rather stimulate virus release.
ESCRT-I mediates FLS2 endosomal sorting and plant immunity.
Robatzek et al., Norwich, United Kingdom. In Plos Genet, 2012
VPS37-1 and VPS28-2 are critical for immunity against bacterial infection through a role in stomatal closure.
VPS37 isoforms differentially modulate the ternary complex formation of ALIX, ALG-2, and ESCRT-I.
Maki et al., Nagoya, Japan. In Biosci Biotechnol Biochem, 2012
The complex, named ESCRT-I, consists of four subunits (TSG101, VPS28, VPS37, and MVB12).
The UBAP1 subunit of ESCRT-I interacts with ubiquitin via a SOUBA domain.
Williams et al., London, United Kingdom. In Structure, 2012
Here we show that ubiquitin associated protein 1 (UBAP1), a subunit of human ESCRT-I, coassembles in a stable 1:1:1:1 complex with Vps23/TSG101, VPS28, and VPS37.
CIIA functions as a molecular switch for the Rac1-specific GEF activity of SOS1.
GeneRIF
Choi et al., Seoul, South Korea. In J Cell Biol, 2011
CIIA functions as a molecular switch for the GEF activity of SOS1, directing this activity toward Rac1.
Multivesicular bodies mature from the trans-Golgi network/early endosome in Arabidopsis.
Schumacher et al., Heidelberg, Germany. In Plant Cell, 2011
The localization of the ESCRT components VPS28, VPS22, and VPS2 at the TGN/EE and MVBs/LEs indicates that the formation of intraluminal vesicles starts already at the TGN/EE.
UBAP1 is a component of an endosome-specific ESCRT-I complex that is essential for MVB sorting.
Woodman et al., Manchester, United Kingdom. In Curr Biol, 2011
Mammalian ESCRT-I comprises TSG101, VPS28, VPS37A-D, and MVB12A/B.
Solution structure of the ESCRT-I complex by small-angle X-ray scattering, EPR, and FRET spectroscopy.
GeneRIF
Hurley et al., Bethesda, United States. In Proc Natl Acad Sci U S A, 2011
Data show that the conformations provide reference points for the structural pathway by which ESCRT-I induces membrane buds.
γ2-Adaptin is functioning in the late endosomal sorting pathway and interacts with ESCRT-I and -III subunits.
GeneRIF
Prange et al., Mainz, Germany. In Biochim Biophys Acta, 2010
Data show that gamma2-adaptin in MVB sorting specifically interacts with the ESCRT subunits Vps28 and CHMP2A.
Recruitment of the ESCRT machinery to a putative seven-transmembrane-domain receptor is mediated by an arrestin-related protein.
GeneRIF
Vincent et al., Madrid, Spain. In Mol Cell Biol, 2010
show that Rim8 coimmunoprecipitates with ESCRT-I subunits Vps23 and Vps28, supporting the idea that binding of Rim8 to Vps23 mediates the association of Rim8 with the ESCRT-I complex.
Budding of filamentous and non-filamentous influenza A virus occurs via a VPS4 and VPS28-independent pathway.
GeneRIF
Digard et al., Cambridge, United Kingdom. In Virology, 2009
Overall, we see no role for the ESCRT pathway in influenza virus budding and the significance of the M1-VPS28 interaction remains to be determined.
Integrated structural model and membrane targeting mechanism of the human ESCRT-II complex.
Hurley et al., Bethesda, United States. In Dev Cell, 2008
ESCRT-II binds to the ESCRT-I VPS28 C-terminal domain subunit through a helix immediately C-terminal to the VPS36-GLUE domain.
Regulation of Tsg101 expression by the steadiness box: a role of Tsg101-associated ligase.
Martin-Serrano et al., London, United Kingdom. In Mol Biol Cell, 2008
We show that VPS28 is a limiting factor, and consequently Tsg101 expression surplus to ESCRT-I function is vulnerable to degradation.
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