An interaction study in mammalian cells demonstrates weak binding of HSPB2 to BAG3, which is regulated by HSPB3 and abrogated by HSPB8
| Autor: | Lonneke Heldens, Ilaria Bigi, Arianna Dorotea Carrà, Jessika Bertacchini, Laura Mediani, Jonathan Vinet, Federica Francesca Morelli, Serena Carra |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Interaction HSP27 Heat-Shock Proteins ALPHA-B-CRYSTALLIN Protein Serine-Threonine Kinases Biology BAG3 Biochemistry Cell Line Myoblasts Weak binding 03 medical and health sciences 0302 clinical medicine HSP22 HSPB8 Heat shock protein medicine Humans Myocyte HEAT-SHOCK PROTEINS Small Heat Shock Proteins Protein Interaction Maps Adaptor Proteins Signal Transducing IDENTIFICATION Competition MUTATIONS MOTOR NEUROPATHY Cardiac muscle alpha-Crystallin B Chain ASSOCIATION Cell Biology DILATED CARDIOMYOPATHY Molecular biology Hsp70 Cell biology HEK293 Cells 030104 developmental biology medicine.anatomical_structure DIFFERENTIATION Small heat shock proteins/HSPBs Weak association Apoptosis Regulatory Proteins 030217 neurology & neurosurgery Function (biology) FORM Molecular Chaperones Protein Binding |
| Zdroj: | Cell stress & chaperones, 22(4), 531-540. SPRINGER |
| ISSN: | 1355-8145 |
| Popis: | The ten mammalian small heat shock proteins (sHSPs/HSPBs) show a different expression profile, although the majority of them are abundant in skeletal and cardiac muscles. HSPBs form hetero-oligomers and homo-oligomers by interacting together and complexes containing, e.g., HSPB2/HSPB3 or HSPB1/HSPB5 have been documented in mammalian cells and muscles. Moreover, HSPB8 associates with the Hsc70/Hsp70 co-chaperone BAG3, in mammalian, skeletal, and cardiac muscle cells. Interaction of HSPB8 with BAG3 regulates its stability and function. Weak association of HSPB5 and HSPB6 with BAG3 has been also reported upon overexpression in cells, supporting the idea that BAG3 might indirectly modulate the function of several HSPBs. However, it is yet unknown whether other HSPBs highly expressed in muscles such as HSPB2 and HSPB3 also bind to BAG3. Here, we report that in mammalian cells, upon overexpression, HSPB2 binds to BAG3 with an affinity weaker than HSPB8. HSPB2 competes with HSPB8 for binding to BAG3. In contrast, HSPB3 negatively regulates HSPB2 association with BAG3. In human myoblasts that express HSPB2, HSPB3, HSPB8, and BAG3, the latter interacts selectively with HSPB8. Combining these data, it supports the interpretation that HSPB8-BAG3 is the preferred interaction. |
| Databáze: | OpenAIRE |
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