| Full text | |
| Author(s): |
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]
Total Authors: 8
|
| Affiliation: | [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
Total Affiliations: 3
|
| Document type: | Review article |
| Source: | FRONTIERS IN CELL AND DEVELOPMENTAL BIOLOGY; v. 9, NOV 19 2021. |
| Web of Science Citations: | 0 |
| Abstract | |
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) | |
| FAPESP's process: | 14/15546-1 - Septins: comparative studies and the correlation between structure and function |
| Grantee: | Richard Charles Garratt |
| Support Opportunities: | Research Projects - Thematic Grants |
| FAPESP's process: | 18/19992-7 - Structural studies of septin heteromeric coiled-coils by nuclear magnetic resonance spectroscopy |
| Grantee: | Italo Augusto Cavini |
| Support Opportunities: | Scholarships in Brazil - Post-Doctoral |
| FAPESP's process: | 20/02897-1 - Septin filaments: structure, polymerization and role in pathologies |
| Grantee: | Richard Charles Garratt |
| Support Opportunities: | Research Projects - Thematic Grants |
| FAPESP's process: | 16/04658-9 - Structural determinants for specific interaction of interfaces G and NC of septins: validating the substitution rules in the assembly of the filament |
| Grantee: | Diego Antonio Leonardo Cabrejos |
| Support Opportunities: | Scholarships in Brazil - Doctorate |
| FAPESP's process: | 19/22000-9 - Septins and flaviviral proteases: a structural analysis |
| Grantee: | Higor Vinícius Dias Rosa |
| Support Opportunities: | Scholarships in Brazil - Master |