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

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 access
Yoon, Yisang, Pitts, Kelly R., McNiven, Mark A.·2001·Molecular Biology of the Cell
DOI 10.1091/mbc.12.9.2894PMC PMC59722
Open this paper in CoChat — free account

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.

Overview

Integrity signals

Registry

Crossref · 10.1091/mbc.12.9.2894

Cites

36 of 36 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Verification

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Citations

Cites

Cited by

Sorted by citations

See all 285

Related

See all

Metadata

Authors
Yoon, Y., Pitts, K. R., & McNiven, M. A.
Affiliations
Mayo Clinic (US)
ORCID
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
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

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review