NDLI: Ubiquitin proteasome pathway-mediated degradation of proteins: effects due to site-specific substrate deamidation.

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Ubiquitin proteasome pathway-mediated degradation of proteins: effects due to site-specific substrate deamidation.

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Ubiquitin proteasome pathway-mediated degradation of proteins: effects due to site-specific substrate deamidation.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Dudek, Edward J. Shang, Fu Wang, Yongting Lampi, Kirsten J. Taylor, Allen Lampi, Jason A. King, Jonathan
Description	Country affiliation: United States Author Affiliation: Dudek EJ ( Laboratory for Nutrition and Vision Research, United States Department of Agriculture Human Nutrition Research Center on Aging at Tufts University, Boston, Massachusetts 02111-1524, USA.)
Abstract	PURPOSE: The accumulation, aggregation, and precipitation of proteins is etiologic for age-related diseases, particularly cataract, because the precipitates cloud the lens. Deamidation of crystallins is associated with protein precipitation, aging, and cataract. Among the roles of the ubiquitin proteasome pathway (UPP) is protein surveillance and maintenance of protein quality. The purpose of this study was to determine whether deamidation can alter clearance of crystallins by the UPP. METHODS: Wild-type (WT) and deamidated crystallins were expressed and (125)I-radiolabeled. Ubiquitination and degradation were monitored separately. RESULTS: For betaB2 crystallins, rates of ubiquitination and adenosine triphosphate-dependent degradation, both indicators of active UPP, occurred in the order Q70E/Q162E>Q162E> Q70E=WT betaB2 using reticulocyte lysate as the source of degradation machinery. Human lens epithelial cell lysates and lens fiber cell lysates also catalyzed ubiquitination but only limited degradation. Supplementation with proteasome failed to enhance degradation. Rates of ubiquitination and degradation of WT and deamidated betaB1 crystallins were rapid and showed little relationship to the site of deamidation using N157D and Q204E mutants. gammaD-Crystallins were not degraded by the UPP. Deamidation altered amine reactivity, circular dichroism spectra, surface hydrophobicity, and thermal stability. CONCLUSIONS: These data demonstrate for the first time that, like mild oxidative stress, deamidation of some proteins makes them preferred substrates for ubiquitination and, in some cells, for UPP-dependent degradation. Failure to properly execute ubiquitination and degrade the ubiquitin-conjugates may explain their accumulation on aging and in cataractogenesis.
ISSN	01460404
e-ISSN	15525783
DOI	10.1167/iovs.09-4087
Journal	Investigative Opthalmology & Visual Science
Issue Number	8
Volume Number	51
Language	English
Publisher	Association for Research in Vision and Ophthalmology
Publisher Date	2010-08-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Ubiquitin-protein Ligase Complexes Physiology Ubiquitin Metabolism Beta-crystallin B Chain Amino Acid Sequence Deamination Electrophoresis, Polyacrylamide Gel Epithelial Cells Lens, Crystalline Molecular Sequence Data Oxidative Stress Substrate Specificity Ubiquitination Chemistry Research Support, N.i.h., Extramural Research Support, Non-u.s. Gov't Research Support, U.s. Gov't, Non-p.h.s. Discipline Ophthalmology
Content Type	Text
Resource Type	Article
Subject	Ophthalmology Sensory Systems Cellular and Molecular Neuroscience

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