ArticleThe Journal of biological chemistry2014
Class I major histocompatibility complex, the trojan horse for secretion of amyloidogenic β2-microglobulin.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Article
- Amyloid Formation by Globular Proteins: The Need to Narrow the Gap BetweenFrontiers in molecular biosciences · 2022Review
- Pathogenic D76N Variant of βBiology · 2021Article
- Investigation of D76N βJournal of the American Society for Mass Spectrometry · 2021Article
- Investigating the Molecular Basis of the Aggregation Propensity of the Pathological D76N Mutant of Beta-2 Microglobulin: Role of the Denatured State.International journal of molecular sciences · 2019Article
- Conformational dynamics in crystals reveal the molecular bases for D76N beta-2 microglobulin aggregation propensity.Nature communications · 2018Article
- HIV-1-Associated Neurocognitive Disorders: Is HLA-C Binding Stability to βFrontiers in neurology · 2018Article
- Rational design of mutations that change the aggregation rate of a protein while maintaining its native structure and stability.Scientific reports · 2016Article
- Historical and Current Concepts of Fibrillogenesis and In vivo Amyloidogenesis: Implications of Amyloid Tissue Targeting.Frontiers in molecular biosciences · 2016Review
- Decoding the Structural Bases of D76N ß2-Microglobulin High Amyloidogenicity through Crystallography and Asn-Scan Mutagenesis.PloS one · 2015Article
- Wild type beta-2 microglobulin and DE loop mutants display a common fibrillar architecture.PloS one · 2015Article
- Bayesian graphical network analyses reveal complex biological interactions specific to Alzheimer's disease.Journal of Alzheimer's disease : JAD · 2015Article
- Energy landscapes of functional proteins are inherently risky.Nature chemical biology · 2014Article
Corrections and comments
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Authors and funding
18 authors.
Funding
Abstract
To form extracellular aggregates, amyloidogenic proteins bypass the intracellular quality control, which normally targets unfolded/aggregated polypeptides. Human D76N β2-microglobulin (β2m) variant is the prototype of unstable and amyloidogenic protein that forms abundant extracellular fibrillar deposits. Here we focus on the role of the class I major histocompatibility complex (MHCI) in the intracellular stabilization of D76N β2m. Using biophysical and structural approaches, we show that the MHCI containing D76N β2m (MHCI76) displays stability, dissociation patterns, and crystal structure comparable with those of the MHCI with wild type β2m. Conversely, limited proteolysis experiments show a reduced protease susceptibility for D76N β2m within the MHCI76 as compared with the free variant, suggesting that the MHCI has a chaperone-like activity in preventing D76N β2m degradation within the cell. Accordingly, D76N β2m is normally assembled in the MHCI and circulates as free plasma species in a transgenic mouse model.
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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.