The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Membrane fission by dynamin: what we know and what we need to know
Open accessAbstract
The large GTPase dynamin is the first protein shown to catalyze membrane fission. Dynamin and its related proteins are essential to many cell functions, from endocytosis to organelle division and fusion, and it plays a critical role in many physiological functions such as synaptic transmission and muscle contraction. Research of the past three decades has focused on understanding how dynamin works. In this review, we present the basis for an emerging consensus on how dynamin functions. Three properties of dynamin are strongly supported by experimental data: first, dynamin oligomerizes into a helical polymer; second, dynamin oligomer constricts in the presence of GTP; and third, dynamin catalyzes membrane fission upon GTP hydrolysis. We present the two current models for fission, essentially diverging in how GTP energy is spent. We further discuss how future research might solve the remaining open questions presently under discussion.
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Citations
Cites
A High Precision Survey of the Molecular Dynamics of Mammalian Clathrin-Mediated Endocytosis
Taylor, M. J., Perrais, D., & Merrifield, C. J. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1000604 · Cited by 754
Self-citationMerrifield, C. J., Perrais, D., & Zenisek, D. (2005) · Cell · doi:10.1016/j.cell.2005.03.015 · Cited by 476 · cited 3×
“In vivo, the fission rate is similar to the fastest in vitro values (5–10 s), and the distribution is also stochastic (Merrifield et al, 2005; Cocucci et al, 2014).”
BackgroundSelf-citationPalmer, C. S., Elgass, K. D., Parton, R. G., Osellame, L. D., Stojanovski, D., & Ryan, M. T. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.479873 · Cited by 301
Crystal structure of nucleotide-free dynamin
Faelber, K., Posor, Y., Gao, S., Held, M., Roske, Y., Schulze, D., Haucke, V., Noé, F., & Daumke, O. (2011) · Nature · doi:10.1038/nature10369 · Cited by 301
Self-citationMeinecke, M., Boucrot, E., Camdere, G., Hon, W.-C., Mittal, R., & McMahon, H. T. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.444869 · Cited by 155
Self-citation
Cited by
Mechanisms of clathrin-mediated endocytosis
Kaksonen, M., & Roux, A. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.132 · Cited by 1,698
Self-citationThe cell biology of mitochondrial membrane dynamics
Giacomello, M., Pyakurel, A., Glytsou, C., & Scorrano, L. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0210-7 · Cited by 1,550
Regulation of Clathrin-Mediated Endocytosis
Mettlen, M., Chen, P.-H., Srinivasan, S., Danuser, G., & Schmid, S. L. (2018) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-062917-012644 · Cited by 614
Self-citationFunction and regulation of the divisome for mitochondrial fission
Kraus, F., Roy, K., Pucadyil, T. J., & Ryan, M. T. (2021) · Nature · doi:10.1038/s41586-021-03214-x · Cited by 445
The Peroxisome-Mitochondria Connection: How and Why?
Fransen, M., Lismont, C., & Walton, P. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18061126 · Cited by 351
“DNM1L is a predominantly cytosolic large guanosine triphosphatase that, upon recruitment to organellar membranes, can self-oligomerize into helices, thereby catalyzing membrane fission and vesicle release in a GTP hydrolysis-dependent manner [50].”
Background
Metadata
- Authors
- Antonny, B., Burd, C., De Camilli, P., Chen, E., Daumke, O., Faelber, K., Ford, M., Frolov, V. A., Frost, A., Hinshaw, J. E., Kirchhausen, T., Kozlov, M. M., Lenz, M., Low, H. H., McMahon, H., Merrifield, C., Pollard, T. D., Robinson, P. J., Roux, A., & Schmid, S.
- Venue
- The EMBO Journal
- Published
- 2016-09-26
- Volume
- 35
- Issue
- 21
- Pages
- 2270-2284
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- OpenAlex
- W2525315911
- Cited by
- 487
- References
- 5
- FWCI
- 36.18
- Type
- journal article
- Language
- en
- Open access
- hybrid
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
