ArticleThe international journal of biochemistry & cell biology2007
Interactive sequences in the stress protein and molecular chaperone human alphaB crystallin recognize and modulate the assembly of filaments.
Article in The international journal of biochemistry & cell biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 74 citations in OpenAlex.
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- Broad Influence of Mutant Ataxin-3 on the Proteome of the Adult Brain, Young Neurons, and Axons Reveals Central Molecular Processes and Biomarkers in SCA3/MJD Using Knock-In Mouse Model.Frontiers in molecular neuroscience · 2021Article
- Friedreich cardiomyopathy is a desminopathy.Free neuropathology · 2021Article
- Red and White Chinook Salmon (Oncorhynchus tshawytscha): Differences in the Transcriptome Profile of Muscle, Liver, and Pylorus.Marine biotechnology (New York, N.Y.) · 2020Article
- Neuromuscular Diseases Due to Chaperone Mutations: A Review and Some New Results.International journal of molecular sciences · 2020Review
- A monoclonal antibody targeted to the functional peptide of αB-crystallin inhibits the chaperone and anti-apoptotic activities.Journal of immunological methods · 2019Article
- The application of gene marker-assisted selection and proteomics for the best meat quality criteria and body measurements in Qinchuan cattle breed.Molecular biology reports · 2018Review
- Intra-vitreal αB crystallin fused to elastin-like polypeptide provides neuroprotection in a mouse model of age-related macular degeneration.Journal of controlled release : official journal of the Controlled Release Society · 2018Article
- Changes in function but not oligomeric size are associated with αB-crystallin lysine substitution.Biochemistry and biophysics reports · 2018Article
- Interaction of small heat shock proteins with light component of neurofilaments (NFL).Cell stress & chaperones · 2017Article
- αB-crystallin is a sensor for assembly intermediates and for the subunit topology of desmin intermediate filaments.Cell stress & chaperones · 2017Article
- The functional roles of the unstructured N- and C-terminal regions in αB-crystallin and other mammalian small heat-shock proteins.Cell stress & chaperones · 2017Article
- Therapeutic potential of α-crystallin.Biochimica et biophysica acta · 2016Review
- Functions of crystallins in and out of lens: roles in elongated and post-mitotic cells.Progress in biophysics and molecular biology · 2014Review
- Reversible and irreversible differentiation of cardiac fibroblasts.Cardiovascular research · 2014Article
- HspB1, HspB5 and HspB4 in Human Cancers: Potent Oncogenic Role of Some of Their Client Proteins.Cancers · 2014Article
- Self-assembly of protein aggregates in ageing disorders: the lens and cataract model.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Molecular chaperones including the small heat shock proteins, alphaB crystallin and sHSP27 participate in the assembly, disassembly, and reorganization of the cytoskeleton during cell development and differentiation. While alphaB crystallin and sHSP27 stabilize and modulate filament assembly and re-organization, the sequences and structural domains mediating interactions between these proteins and filaments are unknown. It is important to define these interactive domains in order to understand differential interactions between chaperones and stable or unfolding filaments and their function in the cellular stress response. Protein pin arrays identified sequences in human alphaB crystallin that selectively interacted with native or partially unfolded filament proteins desmin, glial-fibrillary acidic protein, and actin. Circular dichroism spectroscopy determined differences in the structure of these filaments at 23 and 45 degrees C. Seven alphaB crystallin sequences had stronger interactions with desmin and six sequences had stronger interactions with glial-fibrillary acidic protein at 23 degrees C than at 45 degrees C. The alphaB crystallin sequences (33)LESDLFPTSTSLSPFYLRPPSFLR(56) and (129)DPLTITSSLSSDGV(145) had the strongest interactions with actin at 23 degrees C, while (57)APSWFDTG(64), (111)HGFISREF(118), (145)VNGPRKQVSG(154), and (155)PERTIPITREEK(165) had the strongest interactions with actin at 45 degrees C. The actin interactive sequences of alphaB crystallin overlapped with previously identified alphaB crystallin chaperone sequences and were synthesized to evaluate their effect on the assembly and aggregation of actin. Full-length alphaB crystallin and the core domain chaperone sequence (131)LTITSSLSSDGV(143) promoted actin polymerization at 37 degrees C and inhibited depolymerization and aggregation at 50 degrees C. The results support the hypothesis that interactive domains in alphaB crystallin have multiple functions in stabilizing the cytoskeleton and protecting cytosolic proteins from unfolding.
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