The small heat shock proteins αB-crystallin (HSPB5) and Hsp27 (HSPB1) inhibit the intracellular aggregation of α-synuclein
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چکیده
منابع مشابه
Analysis of the Dominant Effects Mediated by Wild Type or R120G Mutant of αB-crystallin (HspB5) towards Hsp27 (HspB1)
Several human small heat shock proteins (sHsps) are phosphorylated oligomeric chaperones that enhance stress resistance. They are characterized by their ability to interact and form polydispersed hetero-oligomeric complexes. We have analyzed the cellular consequences of the stable expression of either wild type HspB5 or its cataracts and myopathies inducing R120G mutant in growing and oxidative...
متن کاملStructural and functional aspects of hetero-oligomers formed by the small heat shock proteins αB-crystallin and HSP27.
BACKGROUND αB-crystallin and HSP27 are mammalian intracellular small heat shock proteins. RESULTS These proteins exchange subunits in a rapid and temperature-dependent manner. CONCLUSION This facile subunit exchange suggests that differential expression could be used by the cell to regulate the response to stress. SIGNIFICANCE A robust technique defines parameters for the dynamic interact...
متن کاملPreventing α-synuclein aggregation: the role of the small heat-shock molecular chaperone proteins.
Protein homeostasis, or proteostasis, is the process of maintaining the conformational and functional integrity of the proteome. The failure of proteostasis can result in the accumulation of non-native proteins leading to their aggregation and deposition in cells and in tissues. The amyloid fibrillar aggregation of the protein α-synuclein into Lewy bodies and Lewy neuritis is associated with ne...
متن کاملRescue of αB Crystallin (HSPB5) Mutants Associated Protein Aggregation by Co-Expression of HSPB5 Partners
HSPB5 (also called αB-crystallin) is a ubiquitously expressed small heat shock protein. Mutations in HSPB5 have been found to cause cataract, but are also associated with a subgroup of myofibrillar myopathies. Cells expressing each of these HSPB5 mutants are characterized by the appearance of protein aggregates of primarily the mutant HSPB5. Like several members of the HSPB family, HSPB5 can fo...
متن کاملHeterooligomeric complexes formed by human small heat shock proteins HspB1 (Hsp27) and HspB6 (Hsp20).
Formation of heterooligomeric complexes of human small heat shock proteins (sHsp) HspB6 (Hsp20) and HspB1 (Hsp27) was analyzed by means of native gel electrophoresis, analytical ultracentrifugation, chemical cross-linking and size-exclusion chromatography. HspB6 and HspB1 form at least two different complexes with apparent molecular masses 100-150 and 250-300 kDa, and formation of heterooligome...
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ژورنال
عنوان ژورنال: Cell Stress and Chaperones
سال: 2017
ISSN: 1355-8145,1466-1268
DOI: 10.1007/s12192-017-0785-x