Wild-type human γd-crystallin promotes aggregation of its oxidation-mimicking misfolding-prone W42Q mutant

Eugene Serebryany; Jonathan A. King

doi:10.1074/jbc.M114.621581

Wild-type human γd-crystallin promotes aggregation of its oxidation-mimicking misfolding-prone W42Q mutant

Eugene Serebryany
, Jonathan A. King

Physiology and Biophysics

Massachusetts Institute of Technology

Research output: Contribution to journal › Article › peer-review

32 Scopus citations

Abstract

Background: Oxidative damage and destabilizing mutations in γ-crystallins lead to cataract disease. Results: Addition of wild-type γD-crystallin promotes aggregation of the oxidation-mimicking W42Q mutant, yet the wild-type protein escapes coaggregation. Conclusion Wild-type human γD-crystallin can serve as a catalyst for aggregation of its misfolding-prone point mutant. Significance: This finding provides a model of pathology caused by wild-type/mutant or undamaged/damaged protein interactions.

Original language	English
Pages (from-to)	11491-11503
Number of pages	13
Journal	Journal of Biological Chemistry
Volume	290
Issue number	18
DOIs	https://doi.org/10.1074/jbc.M114.621581
State	Published - May 1 2015

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title = "Wild-type human γd-crystallin promotes aggregation of its oxidation-mimicking misfolding-prone W42Q mutant",

abstract = "Background: Oxidative damage and destabilizing mutations in γ-crystallins lead to cataract disease. Results: Addition of wild-type γD-crystallin promotes aggregation of the oxidation-mimicking W42Q mutant, yet the wild-type protein escapes coaggregation. Conclusion Wild-type human γD-crystallin can serve as a catalyst for aggregation of its misfolding-prone point mutant. Significance: This finding provides a model of pathology caused by wild-type/mutant or undamaged/damaged protein interactions.",

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AU - King, Jonathan A.

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N2 - Background: Oxidative damage and destabilizing mutations in γ-crystallins lead to cataract disease. Results: Addition of wild-type γD-crystallin promotes aggregation of the oxidation-mimicking W42Q mutant, yet the wild-type protein escapes coaggregation. Conclusion Wild-type human γD-crystallin can serve as a catalyst for aggregation of its misfolding-prone point mutant. Significance: This finding provides a model of pathology caused by wild-type/mutant or undamaged/damaged protein interactions.

AB - Background: Oxidative damage and destabilizing mutations in γ-crystallins lead to cataract disease. Results: Addition of wild-type γD-crystallin promotes aggregation of the oxidation-mimicking W42Q mutant, yet the wild-type protein escapes coaggregation. Conclusion Wild-type human γD-crystallin can serve as a catalyst for aggregation of its misfolding-prone point mutant. Significance: This finding provides a model of pathology caused by wild-type/mutant or undamaged/damaged protein interactions.

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Wild-type human γd-crystallin promotes aggregation of its oxidation-mimicking misfolding-prone W42Q mutant

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