Cited by 285Cellular transport and secretionLipid Membrane Structure and BehaviorMitochondrial Function and Pathology

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Mammalian Dynamin-like Protein DLP1 Tubulates Membranes

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Yoon, Yisang, Pitts, Kelly R., McNiven, Mark A.·2001·Molecular Biology of the Cell

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Abstract

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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Takei, K., McPherson, P. S., Schmid, S. L., & Camilli, P. V. D. (1995) · Nature · doi:10.1038/374186a0 · Cited by 768
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van der Bliek, A., Redelmeier, T., Damke, H., Tisdale, E. J., Meyerowitz, E. M., & Schmid, S. (1993) · The Journal of Cell Biology · doi:10.1083/jcb.122.3.553 · Cited by 698
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Authors: Yoon, Y., Pitts, K. R., & McNiven, M. A.
Affiliations: Mayo Clinic (US)
ORCID: Yoon, Yisang
McNiven, Mark A.
Venue: Molecular Biology of the Cell
Publisher: American Society for Cell Biology (ASCB)
Published: 2001-09
Volume: 12
Issue: 9
Pages: 2894-2905
ISSN: 1059-1524 (ISSN-L)
1939-4586
DOI: 10.1091/mbc.12.9.2894
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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Mammalian Dynamin-like Protein DLP1 Tubulates Membranes

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