ESCRT-I
VPS28 (Kr.8q24.3), (CIIA nimi esiintyy joissain artikkeleissa ja hiiren homologissa)
- Summary This gene encodes a protein subunit of the ESCRT-I complex (endosomal complexes required for transport), which functions in the transport and sorting of proteins into subcellular vesicles. This complex can also be hijacked to facilitate the budding of enveloped viruses from the cell membrane. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jul 2013]
- Expression Ubiquitous expression in ovary (RPKM 46.0), duodenum (RPKM 44.3) and 25 other tissues See more
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- Orthologs mouse all
- ( Also used name: CIIA , Caspase-activated DNase Inhibitor that Interacts with ASK1 )
Preferred Names
- vacuolar protein sorting-associated protein 28 homolog
- Names
- ESCRT-I complex subunit VPS28
- vacuolar protein sorting 28 homolog
- vacuolar protein sorting 28-like protein
- yeast class E protein Vps28p homolog
Peptide sequence:
Related articles in PubMed
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CIIA negatively regulates the Ras-Erk1/2 signaling pathway through inhibiting the Ras-specific GEF activity of SOS1. Hwang HS, et al. J Cell Sci, 2014 Apr 15. PMID 24522193(CIIA = VPS28 ) https://www.ncbi.nlm.nih.gov/pubmed/24522193/
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Solution structure of the ESCRT-I complex by small-angle X-ray scattering, EPR, and FRET spectroscopy. Boura E, et al. Proc Natl Acad Sci U S A, 2011 Jun 7. PMID 21596998, Free PMC Article ESCRT-I is a heterotetramer of Vps23, Vps28, Vps37, and Mvb12. The crystal structures of the core complex and the ubiquitin E2 variant and Vps28 C-terminal domains have been determined, but internal flexibility has prevented crystallization of intact ESCRT-I. Here we have characterized the structure of ESCRT-I in solution by simultaneous structural refinement against small-angle X-ray scattering and double electron-electron resonance spectroscopy of spin-labeled complexes. An ensemble of at least six structures, comprising an equally populated mixture of closed and open conformations, was necessary to fit all of the data. This structural ensemble was cross-validated against single-molecule FRET spectroscopy, which suggested the presence of a continuum of open states. ESCRT-I in solution thus appears to consist of an approximately 50% population of one or a few related closed conformations, with the other 50% populating a continuum of open conformations. These conformations provide reference points for the structural pathway by which ESCRT-I induces membrane buds.
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