CoChat
Sign Up
Cited by 1,110Mitochondrial Function and PathologyAutophagy in Disease and TherapyCell death mechanisms and regulation

The DOI matches its Crossref record; 62 of the 62 references it cites were found in a registry or an index.

Mff is an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells

Open access
Otera, Hidenori, Wang, Chunxin, Cleland, Megan M., Setoguchi, Kiyoko, Yokota, Sadaki, Youle, Richard J., Mihara, Katsuyoshi·2010·Journal of Cell Biology
DOI 10.1083/jcb.201007152PMC PMC3002033
Open this paper in CoChat — free account

Abstract

The cytoplasmic dynamin-related guanosine triphosphatase Drp1 is recruited to mitochondria and mediates mitochondrial fission. Although the mitochondrial outer membrane (MOM) protein Fis1 is thought to be a Drp1 receptor, this has not been confirmed. To analyze the mechanism of Drp1 recruitment, we manipulated the expression of mitochondrial fission and fusion proteins and demonstrated that (a) mitochondrial fission factor (Mff) knockdown released the Drp1 foci from the MOM accompanied by network extension, whereas Mff overexpression stimulated mitochondrial recruitment of Drp1 accompanied by mitochondrial fission; (b) Mff-dependent mitochondrial fission proceeded independent of Fis1; (c) a Mff mutant with the plasma membrane–targeted CAAX motif directed Drp1 to the target membrane; (d) Mff and Drp1 physically interacted in vitro and in vivo; (e) exogenous stimuli–induced mitochondrial fission and apoptosis were compromised by knockdown of Drp1 and Mff but not Fis1; and (f) conditional knockout of Fis1 in colon carcinoma cells revealed that it is dispensable for mitochondrial fission. Thus, Mff functions as an essential factor in mitochondrial recruitment of Drp1.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1083/jcb.201007152

Cites

62 of 62 references verified0 citation errors · 0 not checkable

Statistics

Figures

Figure 1. Mff siRNA compromises mitochondrial localization of Drp1. (A) Control, Mff, or Fis1 RNAi HeLa cells were analyzed by immunofluorescence microscopy using anti-Drp1 antibody (green) and antimitofilin antibodies (red). Magnified images are shown in insets. (B and C) Mitochondrial network connectivity in either control, Fis1, Mff, or Drp1 RNAi HeLa cells transfected with mito-YFP. In brief, a 2.1-µm circle containing multiple mitochondria was photobleached and monitored for recovery (Fig. S2). The normalized and photobleach corrected curves (B) or mobile fractions (C) represent the mean ± SEM of 60 individual FRAP curves from two independent experiments (30 FRAP curves per experiment). The results were analyzed by the Student’s t test, and p-values are noted on the figure. (D) HeLa cells transfected with the indicated siRNAs were fractionated into cytosol (C) and heavy membrane (HM) fractions, which were analyzed by Western blotting using the indicated antibodies (cytosol/heavy membrane = 1:5 in volume equivalents). Five times the volume equivalent of heavy membrane fraction versus cytosol fraction was loaded to show the difference on mitochondrial recruitment of Drp1 in control (Cont) and Mff RNAi cells. Lactate dehydrogenase (LDH) is a cytosolic marker. (E) Mff RNAi cells were transfected with FLAG-Mff and subjected to immunostaining with anti-Drp1 (green) and anti-FLAG (red) antibodies. Asterisks indicate FLAG-Mff–expressing cells. (F) HeLa cells subjected to the indicated manipulations were fractionated and analyzed as in D. Cytosol/heavy membrane = 1:3 in volume equivalents. (G) FLAG-Mff mutant lacking a TMD (MffΔC) was expressed in HeLa cells. After incubation for 24 h, the cells were fixed and immunostained with anti-FLAG antibody (green) and antimitofilin antibodies (red). Bars, 20 µm.
Figure 1. Mff siRNA compromises mitochondrial localization of Drp1. (A) Control, Mff, or Fis1 RNAi HeLa cells were analyzed by immunofluorescence microscopy using anti-Drp1 antibody (green) and antimitofilin antibodies (red). Magnified images are shown in insets. (B and C) Mitochondrial network connectivity in either control, Fis1, Mff, or Drp1 RNAi HeLa cells transfected with mito-YFP. In brief, a 2.1-µm circle containing multiple mitochondria was photobleached and monitored for recovery (Fig. S2). The normalized and photobleach corrected curves (B) or mobile fractions (C) represent the mean ± SEM of 60 individual FRAP curves from two independent experiments (30 FRAP curves per experiment). The results were analyzed by the Student’s t test, and p-values are noted on the figure. (D) HeLa cells transfected with the indicated siRNAs were fractionated into cytosol (C) and heavy membrane (HM) fractions, which were analyzed by Western blotting using the indicated antibodies (cytosol/heavy membrane = 1:5 in volume equivalents). Five times the volume equivalent of heavy membrane fraction versus cytosol fraction was loaded to show the difference on mitochondrial recruitment of Drp1 in control (Cont) and Mff RNAi cells. Lactate dehydrogenase (LDH) is a cytosolic marker. (E) Mff RNAi cells were transfected with FLAG-Mff and subjected to immunostaining with anti-Drp1 (green) and anti-FLAG (red) antibodies. Asterisks indicate FLAG-Mff–expressing cells. (F) HeLa cells subjected to the indicated manipulations were fractionated and analyzed as in D. Cytosol/heavy membrane = 1:3 in volume equivalents. (G) FLAG-Mff mutant lacking a TMD (MffΔC) was expressed in HeLa cells. After incubation for 24 h, the cells were fixed and immunostained with anti-FLAG antibody (green) and antimitofilin antibodies (red). Bars, 20 µm.CC BY-NC-SA · PubMed Central
Figure 2. Mff and Drp1 colocalize in puncta on mitochondria. (A) Mff overexpression leads to mitochondrial fragmentation. HeLa cells stably expressing Su9-DsRed were transfected with pMff-IRES-GFP-NLS, phFis1-IRES-GFP-NLS, or empty vector and subjected to live imaging by confocal microscopy. Top and bottom images show the cells expressing low and high levels of nuclear GFP, respectively. Typical images are shown in insets at high magnification. (B) Percentages of cells with indicated mitochondrial morphologies in cells (n = 100) transfected with indicated plasmids at 24 h after transfection. Data were collected from three independent experiments and represent the mean ± SD. (C) HeLa cells manipulated as in A were immunostained with anti-Tom22 antibodies (red). The insets show magnified images of the mitochondrial regions. (D) Immunofluorescence microscopy of endogenous Mff in HeLa cells transfected with the indicated siRNA immunostained with anti-Mff (green) and anti-Tom20 (red). (E and F) HeLa cells were immunostained with anti-Drp1 (green) and anti-Mff (red) antibodies. (F) A line scan (shown in the vertical line) plot of relative fluorescence intensities of Mff and Drp1 in the indicated images (same as in E) was analyzed using AxioVision 4.7.1 software (Carl Zeiss, Inc.). The insets in D and E show magnified images of the squared regions.
Figure 2. Mff and Drp1 colocalize in puncta on mitochondria. (A) Mff overexpression leads to mitochondrial fragmentation. HeLa cells stably expressing Su9-DsRed were transfected with pMff-IRES-GFP-NLS, phFis1-IRES-GFP-NLS, or empty vector and subjected to live imaging by confocal microscopy. Top and bottom images show the cells expressing low and high levels of nuclear GFP, respectively. Typical images are shown in insets at high magnification. (B) Percentages of cells with indicated mitochondrial morphologies in cells (n = 100) transfected with indicated plasmids at 24 h after transfection. Data were collected from three independent experiments and represent the mean ± SD. (C) HeLa cells manipulated as in A were immunostained with anti-Tom22 antibodies (red). The insets show magnified images of the mitochondrial regions. (D) Immunofluorescence microscopy of endogenous Mff in HeLa cells transfected with the indicated siRNA immunostained with anti-Mff (green) and anti-Tom20 (red). (E and F) HeLa cells were immunostained with anti-Drp1 (green) and anti-Mff (red) antibodies. (F) A line scan (shown in the vertical line) plot of relative fluorescence intensities of Mff and Drp1 in the indicated images (same as in E) was analyzed using AxioVision 4.7.1 software (Carl Zeiss, Inc.). The insets in D and E show magnified images of the squared regions.CC BY-NC-SA · PubMed Central
Figure 3. Mff interacts with Drp1 both in vivo and in vitro. (A) HeLa cells stably expressing FLAG-Drp1 were transfected with the indicated siRNA and further transfected with phFis1-IRES-GFP-NLS (b) and pMff-IRES-GFP-NLS (c and d). After 24 h, the cells were fixed and immunostained with anti-FLAG antibodies (red). (B) HeLa cells stably expressing FLAG-Drp1 were transfected with HA-Mff. After 24 h, the cells were immunostained with anti-HA antibodies (green) and anti-FLAG antibodies (red). High magnification images (insets) show colocalization of FLAG-Drp1 and HA-Mff. (C) HeLa cells were transfected with Mff siRNA and further transfected with FLAG-Mff-CAAX. The cells were immunostained with antibodies against Drp1 (green) and FLAG (red). Asterisks show FLAG-Mff-CAAX–nonexpressing cells. The insets show magnified images of the squared regions. (D) HeLa cells expressing the indicated proteins were treated with DSP, solubilized either with digitonin buffer (mild condition) or with SDS buffer (stringent condition), and subjected to immunoprecipitation (IP) using anti-FLAG antibody (see Materials and methods). Asterisk shows IgG light chain. IB, immunoblot. (E) Purified proteins were mixed in the indicated combinations and treated with 1 mM DSP. The reaction mixtures were solubilized with 1% Triton X-100 and subjected to immunoprecipitation with anti-Drp1 antibodies. See Materials and methods for details. (F) pMff-IRES-GFP-NLS was cotransfected with HA-WT-Drp1 or HA-Drp1-A395D into HeLa cells, and the cells were analyzed by immunofluorescence microscopy using anti-HA antibodies (red). Note that HA-WT-Drp1, but not HA-Drp1-G395A, was targeted to mitochondria in the Mff-expressing cells. (G) The cells (n = 200) for HA-WT-Drp1 and HA-Drp1-A395D with the cytosol- or mitochondria-localized pattern of Drp1 in A were quantified. vec, vector. (H) The cells treated as in F were analyzed by immunofluorescence microscopy using anti-Tom22. (I) Percentages of cells (n = 200) for HA-WT-Drp1, HA-Drp1-A395D, and HA-Drp1-K38A with the indicated mitochondrial morphology in H. Data were collected from three independent experiments and represent mean ± SD.
Figure 3. Mff interacts with Drp1 both in vivo and in vitro. (A) HeLa cells stably expressing FLAG-Drp1 were transfected with the indicated siRNA and further transfected with phFis1-IRES-GFP-NLS (b) and pMff-IRES-GFP-NLS (c and d). After 24 h, the cells were fixed and immunostained with anti-FLAG antibodies (red). (B) HeLa cells stably expressing FLAG-Drp1 were transfected with HA-Mff. After 24 h, the cells were immunostained with anti-HA antibodies (green) and anti-FLAG antibodies (red). High magnification images (insets) show colocalization of FLAG-Drp1 and HA-Mff. (C) HeLa cells were transfected with Mff siRNA and further transfected with FLAG-Mff-CAAX. The cells were immunostained with antibodies against Drp1 (green) and FLAG (red). Asterisks show FLAG-Mff-CAAX–nonexpressing cells. The insets show magnified images of the squared regions. (D) HeLa cells expressing the indicated proteins were treated with DSP, solubilized either with digitonin buffer (mild condition) or with SDS buffer (stringent condition), and subjected to immunoprecipitation (IP) using anti-FLAG antibody (see Materials and methods). Asterisk shows IgG light chain. IB, immunoblot. (E) Purified proteins were mixed in the indicated combinations and treated with 1 mM DSP. The reaction mixtures were solubilized with 1% Triton X-100 and subjected to immunoprecipitation with anti-Drp1 antibodies. See Materials and methods for details. (F) pMff-IRES-GFP-NLS was cotransfected with HA-WT-Drp1 or HA-Drp1-A395D into HeLa cells, and the cells were analyzed by immunofluorescence microscopy using anti-HA antibodies (red). Note that HA-WT-Drp1, but not HA-Drp1-G395A, was targeted to mitochondria in the Mff-expressing cells. (G) The cells (n = 200) for HA-WT-Drp1 and HA-Drp1-A395D with the cytosol- or mitochondria-localized pattern of Drp1 in A were quantified. vec, vector. (H) The cells treated as in F were analyzed by immunofluorescence microscopy using anti-Tom22. (I) Percentages of cells (n = 200) for HA-WT-Drp1, HA-Drp1-A395D, and HA-Drp1-K38A with the indicated mitochondrial morphology in H. Data were collected from three independent experiments and represent mean ± SD.CC BY-NC-SA · PubMed Central
Figure 4. N-terminal cytosolic region is required for the recruitment of Drp1 to mitochondria. (A) Schematic representation of Mff deletion constructs, and summary of their expression effects on the recruitment and intracellular localization of Drp1 in Mff RNAi cells. Yellow box, TMD from Omp25. Mt, mitochondria. Cyto, cytoplasm. (B) Mff mutants were expressed in Mff RNAi cells and analyzed by immunofluorescence microscopy with anti-Drp1 (green) and anti-FLAG antibodies (red). The insets show magnified images of the mitochondrial regions. (C) Percentages of cells with the indicated mitochondrial morphologies in HeLa cells expressing various Mff deletion mutants as in B. 200 cells in each of three independent experiments were counted. Data represent mean ± SD.
Figure 4. N-terminal cytosolic region is required for the recruitment of Drp1 to mitochondria. (A) Schematic representation of Mff deletion constructs, and summary of their expression effects on the recruitment and intracellular localization of Drp1 in Mff RNAi cells. Yellow box, TMD from Omp25. Mt, mitochondria. Cyto, cytoplasm. (B) Mff mutants were expressed in Mff RNAi cells and analyzed by immunofluorescence microscopy with anti-Drp1 (green) and anti-FLAG antibodies (red). The insets show magnified images of the mitochondrial regions. (C) Percentages of cells with the indicated mitochondrial morphologies in HeLa cells expressing various Mff deletion mutants as in B. 200 cells in each of three independent experiments were counted. Data represent mean ± SD.CC BY-NC-SA · PubMed Central
Figure 5. Mff-induced mitochondrial fission depends on Drp1. (A) FLAG-Mff was transfected in WT or Drp1−/− MEFs. After 36 h, the cells were fixed and immunostained with anti-Tom70 antibodies (green) and anti-FLAG antibodies (red). (B) Percentage of cells with tubular and fragmented mitochondria. Three distinct fields for each 100 cells were counted. Data represent mean ± SD. (C) HeLa cells stably expressing Su9-DsRed were transfected with the indicated siRNA and further transfected with pMff-IRES-GFP-NLS. Live images were obtained by confocal microscopy. (D) HeLa cells in C were subjected to immunoblot analysis using the indicated antibodies with mitofilin as a loading control. Molecular mass is given in kilodaltons. (E) Percentages of cells (n = 100) with the indicated mitochondrial morphologies in mock- and Mff-transfected cells at 24 h after transfection. Data were obtained from three independent experiments and represent mean ± SD.
Figure 5. Mff-induced mitochondrial fission depends on Drp1. (A) FLAG-Mff was transfected in WT or Drp1−/− MEFs. After 36 h, the cells were fixed and immunostained with anti-Tom70 antibodies (green) and anti-FLAG antibodies (red). (B) Percentage of cells with tubular and fragmented mitochondria. Three distinct fields for each 100 cells were counted. Data represent mean ± SD. (C) HeLa cells stably expressing Su9-DsRed were transfected with the indicated siRNA and further transfected with pMff-IRES-GFP-NLS. Live images were obtained by confocal microscopy. (D) HeLa cells in C were subjected to immunoblot analysis using the indicated antibodies with mitofilin as a loading control. Molecular mass is given in kilodaltons. (E) Percentages of cells (n = 100) with the indicated mitochondrial morphologies in mock- and Mff-transfected cells at 24 h after transfection. Data were obtained from three independent experiments and represent mean ± SD.CC BY-NC-SA · PubMed Central
Figure 6. Depletion of Mff, but not hFis1, blocks Opa1 RNAi–induced extensive mitochondrial fragmentation and increased hypersensitivity to apoptosis. (A) HeLa cells stably expressing Su9-DsRed were transfected with the indicated siRNA. Live images were obtained by fluorescence microscopy (a–e magnified images are shown as insets in b and e). EM of these manipulated cells are shown in f–j. (B) Onionlike mitochondrial inner membrane structures in Opa1/Drp1 and Opa1/Mff double knockdown cells. (C) Percentages of cells with the indicated mitochondrial morphologies in various RNAi cells. Data were obtained from 100 cells in each of three independent experiments and represent mean ± SD. (D) HeLa cells were transfected with the indicated siRNA and then treated with actinomycin D in the presence of Z-VAD-FMK. Cells were fixed at the indicated time points, and cytochrome c release was detected by immunostaining. Data were obtained from 300 cells in each of three independent experiments and represent mean ± SD.
Figure 6. Depletion of Mff, but not hFis1, blocks Opa1 RNAi–induced extensive mitochondrial fragmentation and increased hypersensitivity to apoptosis. (A) HeLa cells stably expressing Su9-DsRed were transfected with the indicated siRNA. Live images were obtained by fluorescence microscopy (a–e magnified images are shown as insets in b and e). EM of these manipulated cells are shown in f–j. (B) Onionlike mitochondrial inner membrane structures in Opa1/Drp1 and Opa1/Mff double knockdown cells. (C) Percentages of cells with the indicated mitochondrial morphologies in various RNAi cells. Data were obtained from 100 cells in each of three independent experiments and represent mean ± SD. (D) HeLa cells were transfected with the indicated siRNA and then treated with actinomycin D in the presence of Z-VAD-FMK. Cells were fixed at the indicated time points, and cytochrome c release was detected by immunostaining. Data were obtained from 300 cells in each of three independent experiments and represent mean ± SD.CC BY-NC-SA · PubMed Central
Figure 7. Inhibition of Mff does not affect Bax activation during apoptosis. (A) HeLa cells were transfected with the indicated siRNAs and then treated with actinomycin D (act D) in the presence of Z-VAD-FMK. The cells were immunostained with anti-Bax antibody (green) and anti-Tom22 antibody (red). (B) Time course of Bax activation. HeLa cells (n = 300) in A with mitochondria-targeted Bax were counted in three distinct fields, and data represent mean ± SD. (C) Cells in A were subjected to immunoblot analysis using the indicated antibodies. (D) Mff RNAi HeLa cells in A were fractionated to cytosol (C) and membrane (M) fractions, which were subjected to immunoblot analysis using the indicated antibodies. LDH, lactate dehydrogenase. Molecular mass is given in kilodaltons.
Figure 7. Inhibition of Mff does not affect Bax activation during apoptosis. (A) HeLa cells were transfected with the indicated siRNAs and then treated with actinomycin D (act D) in the presence of Z-VAD-FMK. The cells were immunostained with anti-Bax antibody (green) and anti-Tom22 antibody (red). (B) Time course of Bax activation. HeLa cells (n = 300) in A with mitochondria-targeted Bax were counted in three distinct fields, and data represent mean ± SD. (C) Cells in A were subjected to immunoblot analysis using the indicated antibodies. (D) Mff RNAi HeLa cells in A were fractionated to cytosol (C) and membrane (M) fractions, which were subjected to immunoblot analysis using the indicated antibodies. LDH, lactate dehydrogenase. Molecular mass is given in kilodaltons.CC BY-NC-SA · PubMed Central
Figure 8. Characterization of mitochondrial morphology in Fis1 CKO cells. (A) Comparison of mitochondrial morphology in WT and Fis1 CKO cells immunostained with anti-Tom20 antibody. (B and C) The mitochondrial network connectivity assay showing FRAP curves (B) or mobile fractions (C) from either WT or Fis1−/−-LoxP HCT116 cells was performed as in Fig. 1 (B and C). (D) Mitochondrial fusion rate in either WT or Fis1−/−-LoxP HCT116 cells. A 1.88-µm circle containing multiple mitochondria was activated with a 413-nm laser, and images were acquired at 0, 10, 20, and 30 min after activation using the 488-nm laser. The fraction of remaining activated mitochondria was quantified using MetaMorph software (MDS Analytical Technologies). The mean ± SEM of 23 distinct photoactivated regions is plotted and is representative of three independent experiments. MitoPAGFP, mito-photoactivatable GFP. n.s., not significant. (E) Comparison of mitochondrial fission and fusion protein levels in WT and two sets of Fis1 CKO cells. (F) Drp1 subcellular localization in Fis1 CKO cells. In A and F, magnified images of the squared regions are shown. Bars, 10 µm.
Figure 8. Characterization of mitochondrial morphology in Fis1 CKO cells. (A) Comparison of mitochondrial morphology in WT and Fis1 CKO cells immunostained with anti-Tom20 antibody. (B and C) The mitochondrial network connectivity assay showing FRAP curves (B) or mobile fractions (C) from either WT or Fis1−/−-LoxP HCT116 cells was performed as in Fig. 1 (B and C). (D) Mitochondrial fusion rate in either WT or Fis1−/−-LoxP HCT116 cells. A 1.88-µm circle containing multiple mitochondria was activated with a 413-nm laser, and images were acquired at 0, 10, 20, and 30 min after activation using the 488-nm laser. The fraction of remaining activated mitochondria was quantified using MetaMorph software (MDS Analytical Technologies). The mean ± SEM of 23 distinct photoactivated regions is plotted and is representative of three independent experiments. MitoPAGFP, mito-photoactivatable GFP. n.s., not significant. (E) Comparison of mitochondrial fission and fusion protein levels in WT and two sets of Fis1 CKO cells. (F) Drp1 subcellular localization in Fis1 CKO cells. In A and F, magnified images of the squared regions are shown. Bars, 10 µm.CC BY-NC-SA · PubMed Central
Figure 9. Off-target effect of Fis1 RNAi on mitochondrial morphology. (A) Fis1 and Drp1 protein levels in the indicated RNAi cells. (B) Comparison of mitochondrial morphology in WT, Fis1 CKO, and the indicated RNAi cells. Cells were immunostained with anti–cytochrome c antibody. (C and D) Comparison of mitochondrial morphology in lentivirus-infected control RNAi or Fis1 RNAi HeLa (C) or HCT116 (D) cells immunostained with anti-Tom20 antibody. Knockdown level of each Fis1 shRNA was indicated by Western blotting. The insets show magnified images of the squared regions. Bars, 10 µm.
Figure 9. Off-target effect of Fis1 RNAi on mitochondrial morphology. (A) Fis1 and Drp1 protein levels in the indicated RNAi cells. (B) Comparison of mitochondrial morphology in WT, Fis1 CKO, and the indicated RNAi cells. Cells were immunostained with anti–cytochrome c antibody. (C and D) Comparison of mitochondrial morphology in lentivirus-infected control RNAi or Fis1 RNAi HeLa (C) or HCT116 (D) cells immunostained with anti-Tom20 antibody. Knockdown level of each Fis1 shRNA was indicated by Western blotting. The insets show magnified images of the squared regions. Bars, 10 µm.CC BY-NC-SA · PubMed Central
Figure 10. Mff, but not hFis1, affects peroxisomal morphology. (A) HeLa cells were transfected with the indicated siRNAs, and peroxisome morphology was revealed by immunostaining with anti-PMP70 antibody. (B) Peroxisome morphology in WT and Fis1 CKO cells was detected as in A. The insets show magnified images of the squared regions. Bars, 10 µm.
Figure 10. Mff, but not hFis1, affects peroxisomal morphology. (A) HeLa cells were transfected with the indicated siRNAs, and peroxisome morphology was revealed by immunostaining with anti-PMP70 antibody. (B) Peroxisome morphology in WT and Fis1 CKO cells was detected as in A. The insets show magnified images of the squared regions. Bars, 10 µm.CC BY-NC-SA · PubMed Central

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Cited by

Sorted by citations

See all 1,110

Related

See all

Metadata

Authors
Otera, H., Wang, C., Cleland, M. M., Setoguchi, K., Yokota, S., Youle, R. J., & Mihara, K.
Affiliations
  • Kyushu University (JP)
  • National Institutes of Health (US)
  • Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892 2
  • Nagasaki International University (JP)
Corresponding author
Mihara, Katsuyoshi
ORCID
Venue
Journal of Cell Biology
Publisher
Rockefeller University Press
Published
2010-12-13
Volume
191
Issue
6
Pages
1141-1158
ISSN
  • 0021-9525 (ISSN-L)
  • 1540-8140
DOI
10.1083/jcb.201007152
PMC
PMC3002033
OpenAlex
W2149108521
Cited by
1,110
References
62
Citations by year
2026: 42 · 2025: 67 · 2024: 74 · 2023: 72 · 2022: 88 · 2021: 91 · 2020: 80 · 2019: 69 · 2018: 70 · 2017: 70 · 2016: 77 · 2015: 71 · 2014: 78 · 2013: 60 · 2012: 67
FWCI
20.43
Type
journal article
Language
en
Open access
Licence
cc-by-nc-sa
Locations
  • The Journal of Cell Biology (publishedVersion, cc-by-nc-sa)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
  • PubMed Central (publishedVersion, cc-by-nc-sa)
  • PubMed (publishedVersion)
Funders
National Institutes of Health
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Keywords
Mff, Drp1, mitochondrial fission, mitochondrial recruitment, Fis1, mitochondrial outer membrane, dynamin-related GTPase, mitochondrial fusion, CAAX motif, apoptosis, colon cancer cells, conditional knockout
MeSH terms
Animals, Cells, Cultured, Cytoplasm, Cytoskeletal Proteins, HeLa Cells, Humans, Membrane Proteins, Mitochondria, Down-Regulation, GTP Phosphohydrolases, Mitochondrial Proteins, RNA, Small Interfering

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