ArticleBiology direct2015
Models of buffering of dosage imbalances in protein complexes.
Article in Biology direct, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
- Gene Dosage Sensitivity and Human Genetic Diseases.Journal of inherited metabolic disease · 2025Review
- Integrating protein copy numbers with interaction networks to quantify stoichiometry in clathrin-mediated endocytosis.Scientific reports · 2022Article
- Parent-of-Origin Effects on Seed Size Modify Heterosis Responses inFrontiers in plant science · 2022Article
- Modulation of Global Gene Expression by Aneuploidy and CNV of Dosage Sensitive Regulatory Genes.Genes · 2021Article
- Long QT SyndromeCirculation. Arrhythmia and electrophysiology · 2021Article
- The role of protein complexes in human genetic disease.Protein science : a publication of the Protein Society · 2019Review
- Why haploinsufficiency persists.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Sexual Dimorphism in the Age of Genomics: How, When, Where.Frontiers in cell and developmental biology · 2019Review
- Patterns of Population Variation in Two Paleopolyploid Eudicot Lineages Suggest That Dosage-Based Selection on Homeologs Is Long-Lived.Genome biology and evolution · 2018Article
- Dosage-sensitive genes in evolution and disease.BMC biology · 2017Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundStoichiometric imbalances in macromolecular complexes can lead to altered function. Such imbalances stem from under- or over-expression of a subunit of a complex consequent to a deletion, duplication or regulatory mutation of an allele encoding the relevant protein. In some cases, the phenotypic perturbations induced by such alterations can be subtle or be lacking because nonlinearities in the process of protein complex assembly can provide some degree of buffering.
resultsWe explore with biochemical models of increasing plausibility how buffering can be elicited. Specifically, we analyze the formation of a dimer AB and show that there are particular sets of parameters so that decreasing/increasing the input amount of either A or B translates into a non proportional (buffered) change of AB. The buffer effect also appears in higher-order structures provided that there are intermediate subcomplexes in the assembly process.
conclusionsWe highlight the importance of protein degradation and/or conformational inactivation for buffering to appear. The models sketched here have experimental support but can be further tested with existing biological resources.
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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.