A biochemical view on the septins, a less known component of the cytoskeleton
Author:
Grupp Benjamin1, Gronemeyer Thomas1ORCID
Affiliation:
1. Institute of Molecular Genetics and Cell Biology, Ulm University , James Franck Ring N27, 89081 Ulm , Germany
Abstract
Abstract
The septins are a conserved family of guanine nucleotide binding proteins, often named the fourth component of the cytoskeleton. They self-assemble into non-polar filaments and further into higher ordered structures. Properly assembled septin structures are required for a wide range of indispensable intracellular processes such as cytokinesis, vesicular transport, polarity establishment and cellular adhesion. Septins belong structurally to the P-Loop NTPases. However, unlike the small GTPases like Ras, septins do not mediate signals to effectors through GTP binding and hydrolysis. The role of nucleotide binding and subsequent GTP hydrolysis by the septins is rather controversially debated. We compile here the structural features from the existing septin crystal- and cryo-EM structures regarding protofilament formation, inter-subunit interface architecture and nucleotide binding and hydrolysis. These findings are supplemented with a summary of available biochemical studies providing information regarding nucleotide binding and hydrolysis of fungal and mammalian septins.
Publisher
Walter de Gruyter GmbH
Subject
Clinical Biochemistry,Molecular Biology,Biochemistry
Reference83 articles.
1. Abbey, M., Gaestel, M., and Menon, M.B. (2019). Septins: active GTPases or just GTP‐binding proteins? Cytoskeleton 76: 55–62, https://doi.org/10.1002/cm.21451. 2. Auxier, B., Dee, J., Berbee, M.L., and Momany, M. (2019). Diversity of opisthokont septin proteins reveals structural constraints and conserved motifs. BMC Evol. Biol. 19, https://doi.org/10.1186/s12862-018-1297-8. 3. Bartsch, I., Sandrock, K., Lanza, F., Nurden, P., Hainmann, I., Pavlova, A., Greinacher, A., Tacke, U., Barth, M., Busse, A., et al.. (2011). Deletion of human GP1BB and SEPT5 is associated with Bernard-Soulier syndrome, platelet secretion defect, polymicrogyria, and developmental delay. Thromb. Haemostasis 106: 475–483, https://doi.org/10.1160/th11-05-0305. 4. Baur, J.D., Rösler, R., Wiese, S., Johnsson, N., and Gronemeyer, T. (2018). Dissecting the nucleotide binding properties of the septins from S. cerevisiae. Cytoskeleton 76: 45–54, https://doi.org/10.1002/cm.21484. 5. Beber, A., Taveneau, C., Nania, M., Tsai, F.C., Di Cicco, A., Bassereau, P., Lévy, D., Cabral, J.T., Isambert, H., Mangenot, S., et al.. (2019). Membrane reshaping by micrometric curvature sensitive septin filaments. Nat. Commun. 10: 420, https://doi.org/10.1038/s41467-019-08344-5.
Cited by
4 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
|
|