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Pharmacologically targeting molecular motor promotes mitochondrial fission for anti-cancer

Qian, Yi, Zhao, Meimei, Han, Qinghua, Wang, Jingkang, Liao, Lixi, Yang, Heng, Liu, Dan, Tu, Pengfei, Liang, Hong, Zeng, Kewu·2021·Acta Pharmaceutica Sinica B
DOI 10.1016/j.apsb.2021.01.011PMC PMC8343112
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Graphical abstract Graphical abstract Natural-derived small-molecule J13 restrained the interaction between myosin-9 (MYH9) and actin molecular motor via prompting heat-shock protein A9 (HSPA9) attached to MYH9, resulting in excessive mitochondrial fission with implications for human cancer therapy.
Graphical abstract Graphical abstract Natural-derived small-molecule J13 restrained the interaction between myosin-9 (MYH9) and actin molecular motor via prompting heat-shock protein A9 (HSPA9) attached to MYH9, resulting in excessive mitochondrial fission with implications for human cancer therapy.CC BY-NC-ND · PubMed Central
Figure 1 MYH9-actin molecular motor is a direct cellular target of anti-cancer small-molecule J13. (A) J13 inhibited cell viability of HepG2, SMMC7721, Hepa1-6 and Bel7402 cells (n = 6). (B) J13 induced mitochondrial fission in HepG2 cells. Mitochondrial morphology of HepG2 after J13 treatment was detected by transmission electron microscopy scanning (scale bar = 100 nm). (C) J13 caused mitochondrial fragmentation in HepG2 cells, which was visualized by Mito-tracker staining (scale bar = 10 μm). (D) Inhibition of mitochondrial fission by Mdivi-1 markedly reversed J13-dependent anti-cancer effects by MTT assay (n = 6). (E) J13 induced mitochondrial depolarization by JC-1 staining (scale bar = 25 μm). (F) MYH9 and β-actin were identified as J13-binding proteins using pull-down assay, followed by LC–MS/MS analysis with silver staining. (G) Non-covalent bindings of J13 with MYH9 or β-actin were confirmed by immunoblotting assay with different surfactants NP40, Triton, and SDS. (H) Dissociation constants (KD) of J13 with MYH9 or β-actin were detected by surface plasmon resonance (SPR) analysis. (I) and (J) Cellular thermal shift assays (CETSA) were performed to confirm the binding specificity of J13 with MYH9 or β-actin in cell lysates and living cells. Data are presented as mean ± SD from independent experiments; ∗P < 0.05, ∗∗P < 0.01.
Figure 1 MYH9-actin molecular motor is a direct cellular target of anti-cancer small-molecule J13. (A) J13 inhibited cell viability of HepG2, SMMC7721, Hepa1-6 and Bel7402 cells (n = 6). (B) J13 induced mitochondrial fission in HepG2 cells. Mitochondrial morphology of HepG2 after J13 treatment was detected by transmission electron microscopy scanning (scale bar = 100 nm). (C) J13 caused mitochondrial fragmentation in HepG2 cells, which was visualized by Mito-tracker staining (scale bar = 10 μm). (D) Inhibition of mitochondrial fission by Mdivi-1 markedly reversed J13-dependent anti-cancer effects by MTT assay (n = 6). (E) J13 induced mitochondrial depolarization by JC-1 staining (scale bar = 25 μm). (F) MYH9 and β-actin were identified as J13-binding proteins using pull-down assay, followed by LC–MS/MS analysis with silver staining. (G) Non-covalent bindings of J13 with MYH9 or β-actin were confirmed by immunoblotting assay with different surfactants NP40, Triton, and SDS. (H) Dissociation constants (KD) of J13 with MYH9 or β-actin were detected by surface plasmon resonance (SPR) analysis. (I) and (J) Cellular thermal shift assays (CETSA) were performed to confirm the binding specificity of J13 with MYH9 or β-actin in cell lysates and living cells. Data are presented as mean ± SD from independent experiments; ∗P < 0.05, ∗∗P < 0.01.CC BY-NC-ND · PubMed Central
Figure 2 J13 suppresses direct MYH9–actin interaction to promote mitochondrial fission. (A) MYH9 knock-down reversed J13-dependent cell viability decrease in MTT assay. N.C.: knock-down negative control. (B) J13 suppressed the interaction of MYH9 with β-actin by co-IP assay. (C) Pull-down assay revealed that J13 interacted with actin-binding motif of MYH9. MYH9 F and M: full length MYH9 and mutated MYH9 with a deletion of 23 amino acids (654–676). (D) Docking analysis shows the amino acid residues which may form hydrogen bonds with J13 including ARG165, MET161, ARG240, LYS441, GLN443, GLY444, PHE447, and ASN663. (E) J13 induced allosteric effect of MYH9 by tryptophan fluorescence scanning analysis. (F) J13 suppressed the co-location of ER with mitochondria by double fluorescence staining analysis (ER-tracker, red; Mito-tracker, green; scale bar = 10 μm). (G) ER stress inducers including tunicamycin (Tu), thapsigargin (Th), and calcium ionophore III (CI) exacerbated J13-dependent anti-tumor effect by MTT assay. (H) ER stress inhibitor TUDCA and 4-PBA efficiently reversed J13-induced cell viability decrease in HepG2 cells. All data are presented as mean ± SD, n = 6; ∗P < 0.05, ∗∗P < 0.01.
Figure 2 J13 suppresses direct MYH9–actin interaction to promote mitochondrial fission. (A) MYH9 knock-down reversed J13-dependent cell viability decrease in MTT assay. N.C.: knock-down negative control. (B) J13 suppressed the interaction of MYH9 with β-actin by co-IP assay. (C) Pull-down assay revealed that J13 interacted with actin-binding motif of MYH9. MYH9 F and M: full length MYH9 and mutated MYH9 with a deletion of 23 amino acids (654–676). (D) Docking analysis shows the amino acid residues which may form hydrogen bonds with J13 including ARG165, MET161, ARG240, LYS441, GLN443, GLY444, PHE447, and ASN663. (E) J13 induced allosteric effect of MYH9 by tryptophan fluorescence scanning analysis. (F) J13 suppressed the co-location of ER with mitochondria by double fluorescence staining analysis (ER-tracker, red; Mito-tracker, green; scale bar = 10 μm). (G) ER stress inducers including tunicamycin (Tu), thapsigargin (Th), and calcium ionophore III (CI) exacerbated J13-dependent anti-tumor effect by MTT assay. (H) ER stress inhibitor TUDCA and 4-PBA efficiently reversed J13-induced cell viability decrease in HepG2 cells. All data are presented as mean ± SD, n = 6; ∗P < 0.05, ∗∗P < 0.01.CC BY-NC-ND · PubMed Central
Figure 3 HSPA9 is a crucial MYH9–actin molecular motor substrate protein for controlling mitochondrial dynamics. (A) Schematic illustration of MYH9-binding proteins identification using pull-down coupled with SILAC analysis. (B) HSPA9 was identified as a binding protein of MYH9. (C) J13 promoted the interaction of HSPA9 with MYH9 by co-IP assay. (D) J13 promoted MYH9 interaction with HSPA9 in nucleus. (E) J13 treatment promoted cytosol translocation of HSPA9, and thus increased co-location of MYH9 with HSPA9. (F) J13 induced mitochondrial fragmentation by disrupting COXIV fluorescence distribution. (G) HSPA9 inhibitor MKT-077 (0.5 μmol/L for 24 h) reversed J13-induced cell viability decrease by MTT assay. (H) J13 significantly induced BAX and p-BAD expressions, and inhibited BCL-2 and BCL-XL expressions. (I) J13 induced cytochrome c translocation from mitochondria to cytoplasm. (J) J13 activated caspase-9/3-dependent apoptosis pathway. (K) MYH9 knock-down reversed J13-dependent mitochondrial depolarization (scale bar = 25 μm). (L) MYH9 knock-down rescued J13-dependent cell apoptosis by Hoechst 33258 staining assay (scale bar = 25 μm). All data are presented as mean ± SD from independent experiments (G: n = 6, H–J: n = 3; ∗P < 0.05, ∗∗P < 0.01.
Figure 3 HSPA9 is a crucial MYH9–actin molecular motor substrate protein for controlling mitochondrial dynamics. (A) Schematic illustration of MYH9-binding proteins identification using pull-down coupled with SILAC analysis. (B) HSPA9 was identified as a binding protein of MYH9. (C) J13 promoted the interaction of HSPA9 with MYH9 by co-IP assay. (D) J13 promoted MYH9 interaction with HSPA9 in nucleus. (E) J13 treatment promoted cytosol translocation of HSPA9, and thus increased co-location of MYH9 with HSPA9. (F) J13 induced mitochondrial fragmentation by disrupting COXIV fluorescence distribution. (G) HSPA9 inhibitor MKT-077 (0.5 μmol/L for 24 h) reversed J13-induced cell viability decrease by MTT assay. (H) J13 significantly induced BAX and p-BAD expressions, and inhibited BCL-2 and BCL-XL expressions. (I) J13 induced cytochrome c translocation from mitochondria to cytoplasm. (J) J13 activated caspase-9/3-dependent apoptosis pathway. (K) MYH9 knock-down reversed J13-dependent mitochondrial depolarization (scale bar = 25 μm). (L) MYH9 knock-down rescued J13-dependent cell apoptosis by Hoechst 33258 staining assay (scale bar = 25 μm). All data are presented as mean ± SD from independent experiments (G: n = 6, H–J: n = 3; ∗P < 0.05, ∗∗P < 0.01.CC BY-NC-ND · PubMed Central
Figure 4 J13 inhibits actin-dependent cell migration and angiogenesis. (A) J13 induced allosteric effect of actin in tryptophan fluorescence scanning analysis. (B) J13 induced excessive G-actin assembly which was detected by G-actin polymerization assay. (C) J13 induced G-actin granulation aggregation in cells which was detected by immunofluorescence staining (scale bar = 10 μm). (D) J13 destroyed F-actin cytoskeleton formation which was detected by fluorescent phalloidin staining (scale bar = 25 μm). (E) MYH9 knock-down reversed J13-dependent F-actin cytoskeleton collapse (scale bar = 25 μm). (F) J13 suppressed CAM microvessels formation, cell migration and capillary-like tube formation. All data are presented as mean ± SD from independent experiments performed in triplicate. ∗P < 0.05, ∗∗P < 0.01.
Figure 4 J13 inhibits actin-dependent cell migration and angiogenesis. (A) J13 induced allosteric effect of actin in tryptophan fluorescence scanning analysis. (B) J13 induced excessive G-actin assembly which was detected by G-actin polymerization assay. (C) J13 induced G-actin granulation aggregation in cells which was detected by immunofluorescence staining (scale bar = 10 μm). (D) J13 destroyed F-actin cytoskeleton formation which was detected by fluorescent phalloidin staining (scale bar = 25 μm). (E) MYH9 knock-down reversed J13-dependent F-actin cytoskeleton collapse (scale bar = 25 μm). (F) J13 suppressed CAM microvessels formation, cell migration and capillary-like tube formation. All data are presented as mean ± SD from independent experiments performed in triplicate. ∗P < 0.05, ∗∗P < 0.01.CC BY-NC-ND · PubMed Central
Figure 5 J13 showed anti-tumor effects in vivo. (A) J13 inhibited liver tumor weight growth in H22-bearing ICR mice in vivo by intraperitoneal injection (ip). (B) J13 inhibited liver tumor weight growth of H22-bearing ICR mice in vivo by intragastric administration (ig). (C) J13 inhibited liver tumor size in H22-bearing ICR mice in vivo by intraperitoneal injection (ip). (D) J13 inhibited liver tumor size of H22-bearing ICR mice in vivo by intragastric administration (ig). (E) J13 destroyed cell structure by HE staining (scale bar = 50 μm), decreased Ki67-positive cells number (scale bar = 50 μm), and promoted TUNEL-positive cell apoptosis (scale bar = 20 μm) by ip. (F) J13 destroyed cell structure by HE staining, decreased Ki67-positive cells number, and promoted TUNEL-positive cell apoptosis (scale bar = 20 μm) by ig. (G) J13 reduced CD31-positive cells number and promoted cleaved-caspase 3 (c-CASP3) expression (scale bar = 50 μm) by ip. (H) J13 reduced CD31-positive cells number and promoted c-CASP3 expression (scale bar = 50 μm) by ig. All data are presented as mean ± SD from independent experiments (A–D: n ≥ 8, E–H: n = 3); ∗P < 0.05, ∗∗P < 0.01.
Figure 5 J13 showed anti-tumor effects in vivo. (A) J13 inhibited liver tumor weight growth in H22-bearing ICR mice in vivo by intraperitoneal injection (ip). (B) J13 inhibited liver tumor weight growth of H22-bearing ICR mice in vivo by intragastric administration (ig). (C) J13 inhibited liver tumor size in H22-bearing ICR mice in vivo by intraperitoneal injection (ip). (D) J13 inhibited liver tumor size of H22-bearing ICR mice in vivo by intragastric administration (ig). (E) J13 destroyed cell structure by HE staining (scale bar = 50 μm), decreased Ki67-positive cells number (scale bar = 50 μm), and promoted TUNEL-positive cell apoptosis (scale bar = 20 μm) by ip. (F) J13 destroyed cell structure by HE staining, decreased Ki67-positive cells number, and promoted TUNEL-positive cell apoptosis (scale bar = 20 μm) by ig. (G) J13 reduced CD31-positive cells number and promoted cleaved-caspase 3 (c-CASP3) expression (scale bar = 50 μm) by ip. (H) J13 reduced CD31-positive cells number and promoted c-CASP3 expression (scale bar = 50 μm) by ig. All data are presented as mean ± SD from independent experiments (A–D: n ≥ 8, E–H: n = 3); ∗P < 0.05, ∗∗P < 0.01.CC BY-NC-ND · PubMed Central
Figure 6 MYH9 and HSPA9 expressions are highly associated with poor survival of liver hepatocellular carcinoma (LIHC) patients. (A) MYH9 and HSPA9 had high expression levels in a variety of malignancies [Log2 (TPM+1) ≥2], including liver hepatocellular carcinoma LIHC from TCGA database. (B) The expression levels of MYH9/HSPA9 in LIHC were positively associated with advanced tumor stage determined by TCGA database. (C) MYH9 expression was positively correlated with LIHC patient overall survival (P = 0.013), while HSPA9 expression was positively related with disease free survival of LIHC patients (P = 0.041) based on GEPIA database. (D) A correlation between MYH9 and HSPA9 mRNA expression levels was shown by scatter plot (P = 0.00071) based on two-tailed Pearson's correlation analysis. (E) and (F) The expression levels of MYH9/HSPA9 were markedly increased in LIHC tissues (n = 40) compared to adjacent normal tissues (n = 41), as shown in representative immunohistochemical images (scale bar = 100 μm) and mean staining scores (P < 0.001, nonparametric ANOVA). ∗P < 0.05, ∗∗P < 0.01.
Figure 6 MYH9 and HSPA9 expressions are highly associated with poor survival of liver hepatocellular carcinoma (LIHC) patients. (A) MYH9 and HSPA9 had high expression levels in a variety of malignancies [Log2 (TPM+1) ≥2], including liver hepatocellular carcinoma LIHC from TCGA database. (B) The expression levels of MYH9/HSPA9 in LIHC were positively associated with advanced tumor stage determined by TCGA database. (C) MYH9 expression was positively correlated with LIHC patient overall survival (P = 0.013), while HSPA9 expression was positively related with disease free survival of LIHC patients (P = 0.041) based on GEPIA database. (D) A correlation between MYH9 and HSPA9 mRNA expression levels was shown by scatter plot (P = 0.00071) based on two-tailed Pearson's correlation analysis. (E) and (F) The expression levels of MYH9/HSPA9 were markedly increased in LIHC tissues (n = 40) compared to adjacent normal tissues (n = 41), as shown in representative immunohistochemical images (scale bar = 100 μm) and mean staining scores (P < 0.001, nonparametric ANOVA). ∗P < 0.05, ∗∗P < 0.01.CC BY-NC-ND · PubMed Central

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Metadata

Authors
Qian, Y., Zhao, M., Han, Q., Wang, J., Liao, L., Yang, H., Liu, D., Tu, P., Liang, H., & Zeng, K.
Venue
Acta Pharmaceutica Sinica B
Publisher
Elsevier BV
Published
2021-07
Volume
11
Issue
7
Pages
1853-1866
ISSN
2211-3835
DOI
10.1016/j.apsb.2021.01.011
PMC
PMC8343112
Cited by
22
References
3
Language
en
Update notices
erratum (2024-05-01)
Licence
Funders
  • National Natural Science Foundation of China (81973505, 81773932)
  • National Key Research and Development Program of China (2019YFC1711000, 2019YFC1708902)

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Qian, Y., Zhao, M., Han, Q., Wang, J., Liao, L., Yang, H., Liu, D., Tu, P., Liang, H., & Zeng, K. (2021). Pharmacologically targeting molecular motor promotes mitochondrial fission for anti-cancer. Acta Pharmaceutica Sinica B. https://doi.org/10.1016/j.apsb.2021.01.011