Literature DB >> 11201254

Does post-translational modification influence chaperone-like activity of alpha-crystallin? I. Study on phosphorylation.

A Kamei1, T Hamaguchi, N Matsuura, K Masuda.   

Abstract

It is difficult to isolate derivatives of alpha-crystallin with only one type of post-translational modification, because this protein is subjected to several different types of modification. In the present study using bovine lens proteins, we isolated mono-phosphorylated alphaB-crystallin with no other post-translational modifications. Using this material, we demonstrated that mono-phosphorylation reduced the activity of alphaB-crystallin by approximately 30%. Our results confirmed that investigation of the correlation between chaperone-like activities of alpha-crystallin and post-translational modification is important to understand the mechanism of cataract formation.

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Year:  2001        PMID： 11201254     DOI： 10.1248/bpb.24.96

Source DB:  PubMed          Journal:  Biol Pharm Bull        ISSN： 0918-6158            Impact factor:   2.233


  17 in total

Review 1.  Regulation of αA- and αB-crystallins via phosphorylation in cellular homeostasis.

Authors:  Erin Thornell; Andrew Aquilina
Journal:  Cell Mol Life Sci       Date:  2015-07-26       Impact factor: 9.261

Review 2.  Small heat-shock proteins: important players in regulating cellular proteostasis.

Authors:  Teresa M Treweek; Sarah Meehan; Heath Ecroyd; John A Carver
Journal:  Cell Mol Life Sci       Date:  2014-10-29       Impact factor: 9.261

Review 3.  Biophysical chemistry of the ageing eye lens.

Authors:  Nicholas J Ray
Journal:  Biophys Rev       Date:  2015-08-23

Review 4.  Spatiotemporal changes in the human lens proteome: Critical insights into long-lived proteins.

Authors:  Kevin L Schey; Zhen Wang; Michael G Friedrich; Donita L Garland; Roger J W Truscott
Journal:  Prog Retin Eye Res       Date:  2019-11-06       Impact factor: 21.198

5.  Age-related changes in human crystallins determined from comparative analysis of post-translational modifications in young and aged lens: does deamidation contribute to crystallin insolubility?

Authors:  P A Wilmarth; S Tanner; S Dasari; S R Nagalla; M A Riviere; V Bafna; P A Pevzner; L L David
Journal:  J Proteome Res       Date:  2006-10       Impact factor: 4.466

6.  Phosphorylation-dependent subcellular localization of the small heat shock proteins HspB1/Hsp25 and HspB5/αB-crystallin in cultured hippocampal neurons.

Authors:  Thomas Schmidt; Britta Bartelt-Kirbach; Nikola Golenhofen
Journal:  Histochem Cell Biol       Date:  2012-05-23       Impact factor: 4.304

7.  Succinylation Is a Gain-of-Function Modification in Human Lens αB-Crystallin.

Authors:  Sandip K Nandi; Stefan Rakete; Rooban B Nahomi; Cole Michel; Alexandra Dunbar; Kristofer S Fritz; Ram H Nagaraj
Journal:  Biochemistry       Date:  2019-02-20       Impact factor: 3.162

8.  Mimicking phosphorylation of alphaB-crystallin affects its chaperone activity.

Authors:  Heath Ecroyd; Sarah Meehan; Joseph Horwitz; J Andrew Aquilina; Justin L P Benesch; Carol V Robinson; Cait E Macphee; John A Carver
Journal:  Biochem J       Date:  2007-01-01       Impact factor: 3.857

9.  Identification of in vivo phosphorylation sites of lens proteins from porcine eye lenses by a gel-free phosphoproteomics approach.

Authors:  Shyh-Horng Chiou; Chun-Hao Huang; I-Liang Lee; Yi-Ting Wang; Nai-Yu Liu; Yeou-Guang Tsay; Yu-Ju Chen
Journal:  Mol Vis       Date:  2010-02-24       Impact factor: 2.367

10.  Aggregation and fibrillation of eye lens crystallins by homocysteinylation; implication in the eye pathological disorders.

Authors:  Sima Khazaei; Reza Yousefi; Mohammad-Mehdi Alavian-Mehr
Journal:  Protein J       Date:  2012-12       Impact factor: 2.371
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