The DOI matches its Crossref record; 36 of the 36 references it cites were found in a registry or an index.
Mammalian Dynamin-like Protein DLP1 Tubulates Membranes
Open accessAbstract
Dynamins are large GTPases with mechanochemical properties that are known to constrict and tubulate membranes. A recently identified mammalian dynamin-like protein (DLP1) is essential for the proper cellular distribution of mitochondria and the endoplasmic reticulum in cultured cells. In this study, we investigated the ability of DLP1 to remodel membranes similar to conventional dynamin. We found that the expression of a GTPase-defective mutant, DLP1-K38A, in cultured cells led to the formation of large cytoplasmic aggregates. Electron microscopy (EM) of cells expressing DLP1-K38A revealed that these aggregates were comprised of membrane tubules of a consistent diameter. High-magnification EM revealed the presence of many regular striations along individual membrane tubules, and immunogold labeling confirmed the association of DLP1 with these structures. Biochemical experiments with the use of recombinant DLP1 and labeled GTP demonstrated that DLP1-K38A binds but does not hydrolyze or release GTP. Furthermore, the affinity of DLP1-K38A for membrane is increased compared with wild-type DLP1. To test whether DLP1 could tubulate membrane in vitro, recombinant DLP1 was combined with synthetic liposomes and nucleotides. We found that DLP1 protein alone assembled into sedimentable macromolecular structures in the presence of guanosine-5′-O-(3-thio)triphosphate (GTPγS) but not GTP. EM of the GTPγS-treated DLP1 revealed clusters of stacked helical ring structures. When liposomes were included with DLP1, formation of long membrane tubules similar in size to those formed in vivo was observed. Addition of GTPγS greatly enhanced membrane tubule formation, suggesting the GTP-bound form of DLP1 deforms liposomes into tubules as the DLP1-K38A does in vivo. These results provide the first evidence that the dynamin family member, DLP1, is able to tubulate membranes both in living cells and in vitro. Furthermore, these findings also indicate that despite the limited homology to conventional dynamins (35%) these proteins remodel membranes in a similar manner.
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“Although DRP1 can tubulate the membranes, it cannot complete membrane scission [84].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [84]
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The GTPase superfamily: conserved structure and molecular mechanism
Bourne, H. R., Sanders, D. A., & McCormick, F. (1991) · Nature · doi:10.1038/349117a0 · Cited by 3,392
Induction of mutant dynamin specifically blocks endocytic coated vesicle formation.
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Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding
Hinshaw, J. E., & Schmid, S. L. (1995) · Nature · doi:10.1038/374190a0 · Cited by 824
The dynamin-related GTPase Dnm1 regulates mitochondrial fission in yeast
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Tubular membrane invaginations coated by dynamin rings are induced by GTP-γS in nerve terminals
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Dynamin-mediated Internalization of Caveolae
Henley, J. R., Krueger, E. W. A., Oswald, B. J., & McNiven, M. A. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.141.1.85 · Cited by 767
Self-citationA Human Dynamin-related Protein Controls the Distribution of Mitochondria
Смирнова, Е. А., Shurland, D., Ryazantsev, S. N., & van der Bliek, A. M. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.2.351 · Cited by 734
Mutations in human dynamin block an intermediate stage in coated vesicle formation
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Dynamin Undergoes a GTP-Dependent Conformational Change Causing Vesiculation
Sweitzer, S. M., & Hinshaw, J. E. (1998) · Cell · doi:10.1016/s0092-8674(00)81207-6 · Cited by 682
C. elegans Dynamin-Related Protein DRP-1 Controls Severing of the Mitochondrial Outer Membrane
Labrousse, A. M., Zappaterra, M. D., Rube, D. A., & van der Bliek, A. M. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80391-3 · Cited by 670
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Friedman, J. R., Lackner, L. L., West, M., DiBenedetto, J. R., Nunnari, J., & Voeltz, G. K. (2011) · Science · doi:10.1126/science.1207385 · Cited by 2,072
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Metadata
- Authors
- Yoon, Y., Pitts, K. R., & McNiven, M. A.
- Affiliations
- Mayo Clinic (US)
- Venue
- Molecular Biology of the Cell
- Published
- 2001-09
- Volume
- 12
- Issue
- 9
- Pages
- 2894-2905
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- PMC
- PMC59722
- OpenAlex
- W2124540225
- Cited by
- 285
- References
- 36
- Citations by year
- 2026: 3 · 2025: 6 · 2024: 5 · 2023: 5 · 2022: 4 · 2021: 9 · 2020: 8 · 2019: 12 · 2018: 10 · 2017: 14 · 2016: 12 · 2015: 14 · 2014: 11 · 2013: 15 · 2012: 16
- FWCI
- 3.40
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular Biology of the Cell (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5k01dk002648-03)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK44650, DK 02648, R37DK044650, R01DK044650)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Keywords
- dynamin-like protein, membrane tubulation, GTPase activity, GTP hydrolysis, GTP gamma S, membrane remodeling, mitochondrial distribution, cytoplasmic aggregates, liposome deformation
- MeSH terms
- Animals, Cell Line, Cell Membrane, Guanosine Triphosphate, Cricetinae, Hydrolysis, Liposomes, Mammals, Membrane Fusion, Microscopy, Electron, Microscopy, Fluorescence, Microtubule-Associated Proteins, Proteins, Time Factors, Amino Acid Substitution, GTP Phosphohydrolases, Mitochondrial Proteins, Dynamins
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