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


Ecm29, ecm29p, KIAA0368
Top mentioned proteins: Ubiquitin, CAN, fibrillin-1, ATPase, Inactive
Papers on Ecm29
Stage-Dependent Axon Transport of Proteasomes Contributes to Axon Development.
Cheng et al., Taipei, Taiwan. In Dev Cell, Dec 2015
Such an effect occurred through phosphorylation of a dynein-interacting proteasome adaptor protein Ecm29.
MicroRNA expression signature of castration-resistant prostate cancer: the microRNA-221/222 cluster functions as a tumour suppressor and disease progression marker.
Seki et al., Chiba, Japan. In Br J Cancer, Oct 2015
Ecm29 was directly regulated by the miR-221/222 cluster in PCa cells.
Centrosomes at M phase act as a scaffold for the accumulation of intracellular ubiquitinated proteins.
Nakanishi et al., Tokyo, Japan. In Cell Cycle, 2013
RNA interference suppression of Ecm29, which inhibits proteasome activity, decreased the accumulation of ubiquitinated proteins in the centrosomes.
The proteasome-associated protein Ecm29 inhibits proteasomal ATPase activity and in vivo protein degradation by the proteasome.
Roelofs et al., In J Biol Chem, 2013
The proteasome-associated protein Ecm29, however, has no ubiquitin-binding or modifying activity, and its direct effect on substrate degradation is unclear.
Depletion of the 26S proteasome adaptor Ecm29 increases Toll-like receptor 3 signaling.
Bowles et al., Salt Lake City, United States. In Sci Signal, 2013
We found that depletion of extracellular mutant 29 (Ecm29), an adaptor protein that binds to a subset of 26S proteasomes (Ecm proteasomes), increased the abundance of TLR3 in human embryonic kidney-293 and HeLa cells.
Loss of Rpt5 protein interactions with the core particle and Nas2 protein causes the formation of faulty proteasomes that are inhibited by Ecm29 protein.
Roelofs et al., Manhattan, United States. In J Biol Chem, 2011
Loss of Rpt5 protein interactions with the core particle and Nas2 protein causes the formation of faulty proteasomes that are inhibited by Ecm29 protein.
Structural defects in the regulatory particle-core particle interface of the proteasome induce a novel proteasome stress response.
Finley et al., Boston, United States. In J Biol Chem, 2011
Incorporation of immature CP into the proteasome depended on a proteasome-associated protein, Ecm29.
Not4 E3 ligase contributes to proteasome assembly and functional integrity in part through Ecm29.
Collart et al., Genève, Switzerland. In Mol Cell Biol, 2011
results characterize Ecm29 as a proteasome chaperone whose appropriate interaction with the proteasome requires Not4
A protein interaction network for Ecm29 links the 26 S proteasome to molecular motors and endosomal components.
Rechsteiner et al., Salt Lake City, United States. In J Biol Chem, 2010
Ecm29 serves as an adaptor for coupling 26 S proteasomes to specific cellular compartments.
Ecm29 fulfils quality control functions in proteasome assembly.
Enenkel et al., Berlin, Germany. In Mol Cell, 2010
We sought for proteins that regulate final steps of RP-CP assembly in yeast and found Ecm29, a conserved HEAT-like repeat protein.
Effects of ethanol on the proteasome interacting proteins.
Bardag-Gorce, Los Angeles, United States. In World J Gastroenterol, 2010
Interaction of the proteasome with Ecm29 and with deubiquitinating enzymes Rpn11, UCH37, and Usp14 has been found to decrease.
Regulation of the 26S proteasome complex during oxidative stress.
Huang et al., Irvine, United States. In Sci Signal, 2009
Studies indicate that deletion of ECM29 prevented the disassembly of the 26S proteasome in response to oxidative stress, and ecm29 mutants were more sensitive to HO than were wild-type cells.
Chronic ethanol feeding affects proteasome-interacting proteins.
Bardag-Gorce et al., Toulouse, France. In Proteomics, 2009
20S proteasome and most 19S subunits were however not changed but Ecm29, a protein known to stabilize the interactions between the 20S and its activators, was decreased in the isolated ethanol proteasome fractions.
Stability of the proteasome can be regulated allosterically through engagement of its proteolytic active sites.
Finley et al., Boston, United States. In Nat Struct Mol Biol, 2007
However, this nucleotide is dispensable for gating of the CP channel, provided that the CP-RP complex is preserved by the Ecm29 protein.
Characterization of mammalian Ecm29, a 26 S proteasome-associated protein that localizes to the nucleus and membrane vesicles.
Rechsteiner et al., Salt Lake City, United States. In J Biol Chem, 2005
Ecm29 protein serves to couple the 26 S proteasome to secretory compartments engaged in quality control and to other sites of enhanced proteolysis
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