ArticleMolecular biology of the cell2003
Dislocation of a type I membrane protein requires interactions between membrane-spanning segments within the lipid bilayer.
Article in Molecular biology of the cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
24 citing papers in PubMed, 38 citations in OpenAlex.
- Calnexin reveals a sugar-free taste within the lipid bilayer.The EMBO journal · 2022Article
- A slowly cleaved viral signal peptide acts as a protein-integral immune evasion domain.Nature communications · 2021Article
- HLA-B locus products resist degradation by the human cytomegalovirus immunoevasin US11.PLoS pathogens · 2019Article
- Battle between Host Immune Cellular Responses and HCMV Immune Evasion.International journal of molecular sciences · 2019Review
- Human cytomegalovirus evades antibody-mediated immunity through endoplasmic reticulum-associated degradation of the FcRn receptor.Nature communications · 2019Article
- Identifying the ERAD ubiquitin E3 ligases for viral and cellular targeting of MHC class I.Molecular immunology · 2015Review
- Classical and non-classical MHC I molecule manipulation by human cytomegalovirus: so many targets—but how many arrows in the quiver?Cellular & molecular immunology · 2015Review
- The influenza virus neuraminidase protein transmembrane and head domains have coevolved.Journal of virology · 2015Article
- A high-coverage shRNA screen identifies TMEM129 as an E3 ligase involved in ER-associated protein degradation.Nature communications · 2014Article
- Article
- Diverse immune evasion strategies by human cytomegalovirus.Immunologic research · 2012Review
- Human cytomegalovirus US3 modulates destruction of MHC class I molecules.Molecular immunology · 2012Article
- The p97 ATPase dislocates MHC class I heavy chain in US2-expressing cells via a Ufd1-Npl4-independent mechanism.The Journal of biological chemistry · 2010Article
- The otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ER.Molecular cell · 2009Article
- TRAM1 participates in human cytomegalovirus US2- and US11-mediated dislocation of an endoplasmic reticulum membrane glycoprotein.The Journal of biological chemistry · 2009Article
- SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteins.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- A bipartite trigger for dislocation directs the proteasomal degradation of an endoplasmic reticulum membrane glycoprotein.The Journal of biological chemistry · 2008Article
- SEL1L, the homologue of yeast Hrd3p, is involved in protein dislocation from the mammalian ER.The Journal of cell biology · 2006Article
- A short isoform of human cytomegalovirus US3 functions as a dominant negative inhibitor of the full-length form.Journal of virology · 2006Article
- Antigen presentation and the ubiquitin-proteasome system in host-pathogen interactions.Advances in immunology · 2006Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The human cytomegalovirus gene product US11 causes rapid degradation of class I major histocompatibility complex (MHCI) heavy chains by inducing their dislocation from the endoplasmic reticulum (ER) and subsequent degradation by the proteasome. This set of reactions resembles the endogenous cellular quality control pathway that removes misfolded or unassembled proteins from the ER. We show that the transmembrane domain (TMD) of US11 is essential for MHCI heavy chain dislocation, but dispensable for MHCI binding. A Gln residue at position 192 in the US11 TMD is crucial for the ubiquitination and degradation of MHCI heavy chains. Cells that express US11 TMD mutants allow formation of MHCI-beta2m complexes, but their rate of egress from the ER is significantly impaired. Further mutagenesis data are consistent with the presence of an alpha-helical structure in the US11 TMD essential for MHCI heavy chain dislocation. The failure of US11 TMD mutants to catalyze dislocation is a unique instance in which a polar residue in the TMD of a type I membrane protein is required for that protein's function. Targeting of MHCI heavy chains for dislocation by US11 thus requires the formation of interhelical hydrogen bonds within the ER membrane.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.