The DOI matches its Crossref record; 38 of the 38 references it cites were found in a registry or an index.
Hsp90 as a capacitor for morphological evolution
Abstract
The heat-shock protein Hsp90 supports diverse but specific signal transducers and lies at the interface of several developmental pathways. We report here that when Drosophila Hsp90 is mutant or pharmacologically impaired, phenotypic variation affecting nearly any adult structure is produced, with specific variants depending on the genetic background and occurring both in laboratory strains and in wild populations. Multiple, previously silent, genetic determinants produced these variants and, when enriched by selection, they rapidly became independent of the Hsp90 mutation. Therefore, widespread variation affecting morphogenic pathways exists in nature, but is usually silent; Hsp90 buffers this variation, allowing it to accumulate under neutral conditions. When Hsp90 buffering is compromised, for example by temperature, cryptic variants are expressed and selection can lead to the continued expression of these traits, even when Hsp90 function is restored. This provides a plausible mechanism for promoting evolutionary change in otherwise entrenched developmental processes.
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In the citing paper
“Hence Hsp90 has acted as an evolutionary capacitor during eukaryotic evolution19-21.”
From Fungal Hsp90: a biological transistor that tunes cellular outputs to thermal inputs (2012) · cites this paper as [19]
In the citing paper
“First, Hsp90 can buffer the effects of genetic or epigenetic variation, keeping it silent until released when the chaperone reservoir is compromised in response to stress.”
From Fungal Hsp90: a biological transistor that tunes cellular outputs to thermal inputs (2012) · cites this paper as [19]
In the citing paper
“This role as a capacitor for variation has been observed in diverse eukaryotes including flies, plants, and fungi18,19,129-134.”
From Fungal Hsp90: a biological transistor that tunes cellular outputs to thermal inputs (2012) · cites this paper as [19]
Citations
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Flagged first, then by citations
Research works printed but not linked: 1
- Xu, Y., Singer, M. & Lindquist, S. Maturation of c-src as a kinase and as a substrate is dependent on Hsp90. Proc. Natl Acad. Sci. USA (in the press).
Cited by
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Items 1,001–1,003 of 1,003
Selective Breeding for an Infantile Phenotype (Isolation Calling)
Brunelli, S. A., & Hofer, M. A. (2001) · Handbook of Behavioral Neurobiology · doi:10.1007/978-1-4615-1209-7_12 · Cited by 9
- Self-citation
Sánchez (2002) · doi:10.1379/1466-1268(2002)007
Metadata
- Authors
- Rutherford, S. L., & Lindquist, S.
- Affiliations
- Howard Hughes Medical Institute (US)
- Venue
- Nature
- Published
- 1998-11
- Volume
- 396
- Issue
- 6709
- Pages
- 336-342
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1554180547
- Cited by
- 2,270
- References
- 38
- Citations by year
- 2026: 45 · 2025: 57 · 2024: 53 · 2023: 58 · 2022: 60 · 2021: 54 · 2020: 56 · 2019: 86 · 2018: 95 · 2017: 77 · 2016: 84 · 2015: 93 · 2014: 104 · 2013: 108 · 2012: 93
- FWCI
- 18.89
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Evolution and Genetic Dynamics
- Life Sciences › Agricultural and Biological Sciences › Ecology, Evolution, Behavior and Systematics › Morphological variations and asymmetry
- Keywords
- HSP90, morphological evolution, cryptic genetic variation, Drosophila, developmental pathways, signal transduction, genetic background effects, temperature effects, morphological variation
- MeSH terms
- Animals, Drosophila, Heat-Shock Proteins, Models, Genetic, Mutation, Phenotype, Temperature, Genetic Variation, HSP90 Heat-Shock Proteins, Directed Molecular Evolution, Drosophila Proteins
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