| Texto completo | |
| Autor(es): |
Cavini, Italo A.
[1]
;
Leonardo, Diego A.
[1]
;
Rosa, Higor V. D.
[1]
;
Castro, Danielle K. S. V.
[1, 2]
;
D'Muniz Pereira, Humberto
[1]
;
Valadares, Napoleao F.
[3]
;
Araujo, Ana P. U.
[1]
;
Garratt, Richard C.
[1]
Número total de Autores: 8
|
| Afiliação do(s) autor(es): | [1] Univ Sao Paulo, Sao Carlos Inst Phys, Sao Carlos - Brazil
[2] Univ Sao Paulo, Sao Carlos Inst Chem, Sao Carlos - Brazil
[3] Univ Brasilia, Dept Cellular Biol, Brasilia, DF - Brazil
Número total de Afiliações: 3
|
| Tipo de documento: | Artigo de Revisão |
| Fonte: | FRONTIERS IN CELL AND DEVELOPMENTAL BIOLOGY; v. 9, NOV 19 2021. |
| Citações Web of Science: | 0 |
| Resumo | |
In order to fully understand any complex biochemical system from a mechanistic point of view, it is necessary to have access to the three-dimensional structures of the molecular components involved. Septins and their oligomers, filaments and higher-order complexes are no exception. Indeed, the spontaneous recruitment of different septin monomers to specific positions along a filament represents a fascinating example of subtle molecular recognition. Over the last few years, the amount of structural information available about these important cytoskeletal proteins has increased dramatically. This has allowed for a more detailed description of their individual domains and the different interfaces formed between them, which are the basis for stabilizing higher-order structures such as hexamers, octamers and fully formed filaments. The flexibility of these structures and the plasticity of the individual interfaces have also begun to be understood. Furthermore, recently, light has been shed on how filaments may bundle into higher-order structures by the formation of antiparallel coiled coils involving the C-terminal domains. Nevertheless, even with these advances, there is still some way to go before we fully understand how the structure and dynamics of septin assemblies are related to their physiological roles, including their interactions with biological membranes and other cytoskeletal components. In this review, we aim to bring together the various strands of structural evidence currently available into a more coherent picture. Although it would be an exaggeration to say that this is complete, recent progress seems to suggest that headway is being made in that direction. (AU) | |
| Processo FAPESP: | 14/15546-1 - Septinas: estudos comparativos visando correlacionar estrutura e função |
| Beneficiário: | Richard Charles Garratt |
| Modalidade de apoio: | Auxílio à Pesquisa - Temático |
| Processo FAPESP: | 18/19992-7 - Estudos estruturais dos coiled-coils heteroméricos de septinas por espectroscopia de ressonância magnética nuclear e cristalografia de raios-X |
| Beneficiário: | Italo Augusto Cavini |
| Modalidade de apoio: | Bolsas no Brasil - Pós-Doutorado |
| Processo FAPESP: | 20/02897-1 - Filamentos de septinas: estrutura, polimerização e atuação em patologias |
| Beneficiário: | Richard Charles Garratt |
| Modalidade de apoio: | Auxílio à Pesquisa - Temático |
| Processo FAPESP: | 16/04658-9 - Determinantes estruturais para a especificidade de interação nas interfaces G e NC de septinas: validando as regras de substituição na montagem do filamento |
| Beneficiário: | Diego Antonio Leonardo Cabrejos |
| Modalidade de apoio: | Bolsas no Brasil - Doutorado |
| Processo FAPESP: | 19/22000-9 - Septinas e proteases de flavivirus: uma análise estrutural |
| Beneficiário: | Higor Vinícius Dias Rosa |
| Modalidade de apoio: | Bolsas no Brasil - Mestrado |