Characterization of type III intermediate filament regulatory protein target epitopes: S-100 (β and/or α) binds the N-terminal head domain; annexin II2-p112 binds the rod domain
| Autor: | Marisa Garbuglia, Rosario Donato, Gordon A. Jamieson, Ruth V.W. Dimlich, Marco Verzini |
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| Rok vydání: | 1996 |
| Předmět: |
Protein Denaturation
Swine Protein subunit Intermediate Filaments Succinimides macromolecular substances S100 Calcium Binding Protein beta Subunit Biology Epitope Desmin chemistry.chemical_compound Annexin Glial Fibrillary Acidic Protein Animals Urea Nerve Growth Factors Intermediate filament Molecular Biology Annexin A2 Binding Sites Glial fibrillary acidic protein GFAP Type III Intermediate Filament S100 Proteins Cell Biology musculoskeletal system Molecular biology Peptide Fragments Cell biology Molecular Weight Cross-Linking Reagents nervous system chemistry biology.protein Calcium Cattle PMSF Peptides Chickens Biomarkers S-100 protein Protein Binding |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1313(3):268-276 |
| ISSN: | 0167-4889 |
| DOI: | 10.1016/0167-4889(96)00099-7 |
| Popis: | We have investigated the interaction of S-100 proteins (beta and/or alpha) and annexin II2-p11(2) with glial fibrillary acidic protein (GFAP) and desmin to have further information on the mechanisms whereby S-100 proteins and annexin II2-p11(2) affect assembly/disassembly of GFAP and desmin intermediate filaments (IFs). Analyses were conducted on either native IF subunits, GFAP or desmin rod domain, or headless GFAP or desmin. Our data indicate that: (i) S-100 proteins bind to GFAP and desmin N-terminal head domain; (ii) annexin II2-p11(2) binds to GFAP rod domain; (iii) annexin II2-p11(2) does not interact with desmin nor affects desmin assembly. The present data suggest that the ability of S-100 proteins to inhibit GFAP and desmin assemblies and to promote the disassembly of preformed GFAP and desmin IFs depends on occupation of a site on the N-terminal head domain of these IF subunit. It is known that the N-terminal head domain is critical for the progression from the stage of GFAP and desmin dimers/tetramers to that of large oligomers. On the other hand, the ability of annexin II2-p11(2) to stimulate GFAP assembly under conditions where this latter is normally hampered (e.g., at alkaline pH values) might depend on annexin II2-p11(2)-induced changes in the structure of GFAP rod domain, possibly as a consequence of charge modifications. By contrast, the inability of annexin II2-p11(2) to bind to desmin would depend on desmin resistance to charge modifications. |
| Databáze: | OpenAIRE |
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