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A Schematic of the desmosome under tension. The N-terminal region of DP transitions from a closed conformation to an open conformation. B Representative STED images of DPC (green) <t>and</t> <t>Dsg2</t> (red) at the cell border for WT and K19-KO cells. Scale bar: 500 nm. C Representative STED images of <t>DPN</t> (green) and Dsg2 (red) at the cell border for WT and K19-KO cells. Scale bar: 500 nm. D Quantification of desmosome half-unit widths (Dsg2-DPC distance) from WT and K19-KO cells. n = 1260 (WT), 1010 (K19-KO); N = 3. Two-sided Mann–Whitney’s U test; P = 1.542E–66, *** P < 0.001. The distances between Dsg2 and DPC are significantly greater in the WT compared to the K19-KO cells. E Quantification of desmosome half-unit widths (Dsg2-DPN distance) from WT and K19-KO cells. n = 692 (WT), 826 (K19-KO); N = 3. Two-sided Mann–Whitney’s U test; ns, P > 0.05. The Dsg2-DPN distance is similar in both cell lines. F The mean values from the results in D and E are summarized in the bar chart to compare the DP length (DPN - DPC distance) between the WT and K19-KO cells. The DP length is 66 nm for the WT and 33 nm for the K19-KO, indicating that DP extends 33 nm in the WT cells. G The entire plakin domain structure predicted by AlphaFold2 suggests a U-shape conformation in the absence of force. Two common electrostatic interactions (R592-N744 and K444-E858) observed in all 3 MD simulations (below) are shown. H During the MD simulations, 10 to 15 hydrogen bonds were formed between the plakin domain’s long arm (SR3-4 and SR5-6) and short arm (SR7-8 and SR8-CT). I During the SMD simulations, the distance between the plakin domain’s C-terminus and N-terminus increased by 30~33 nm. This elongation correlates with the distance change experimentally measured in Fig. . J Comparison of the plakin domain structure at the start (left) and at the end (right) of the SMD simulation. The structures show that the plakin domain was elongated by the pulling force without significant secondary structure unfolding. All boxplots show median, 25th and 75th percentile with whiskers reaching the last data point within 1.5× interquartile range. Data points outside this range are plotted individually as outliers. The number of data points n represents the number of line scans across the desmosomes.
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A Schematic of the desmosome under tension. The N-terminal region of DP transitions from a closed conformation to an open conformation. B Representative STED images of DPC (green) <t>and</t> <t>Dsg2</t> (red) at the cell border for WT and K19-KO cells. Scale bar: 500 nm. C Representative STED images of <t>DPN</t> (green) and Dsg2 (red) at the cell border for WT and K19-KO cells. Scale bar: 500 nm. D Quantification of desmosome half-unit widths (Dsg2-DPC distance) from WT and K19-KO cells. n = 1260 (WT), 1010 (K19-KO); N = 3. Two-sided Mann–Whitney’s U test; P = 1.542E–66, *** P < 0.001. The distances between Dsg2 and DPC are significantly greater in the WT compared to the K19-KO cells. E Quantification of desmosome half-unit widths (Dsg2-DPN distance) from WT and K19-KO cells. n = 692 (WT), 826 (K19-KO); N = 3. Two-sided Mann–Whitney’s U test; ns, P > 0.05. The Dsg2-DPN distance is similar in both cell lines. F The mean values from the results in D and E are summarized in the bar chart to compare the DP length (DPN - DPC distance) between the WT and K19-KO cells. The DP length is 66 nm for the WT and 33 nm for the K19-KO, indicating that DP extends 33 nm in the WT cells. G The entire plakin domain structure predicted by AlphaFold2 suggests a U-shape conformation in the absence of force. Two common electrostatic interactions (R592-N744 and K444-E858) observed in all 3 MD simulations (below) are shown. H During the MD simulations, 10 to 15 hydrogen bonds were formed between the plakin domain’s long arm (SR3-4 and SR5-6) and short arm (SR7-8 and SR8-CT). I During the SMD simulations, the distance between the plakin domain’s C-terminus and N-terminus increased by 30~33 nm. This elongation correlates with the distance change experimentally measured in Fig. . J Comparison of the plakin domain structure at the start (left) and at the end (right) of the SMD simulation. The structures show that the plakin domain was elongated by the pulling force without significant secondary structure unfolding. All boxplots show median, 25th and 75th percentile with whiskers reaching the last data point within 1.5× interquartile range. Data points outside this range are plotted individually as outliers. The number of data points n represents the number of line scans across the desmosomes.
Antidesmoplakin, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/antidesmoplakin/product/Proteintech
Average 93 stars, based on 1 article reviews
antidesmoplakin - by Bioz Stars, 2026-05
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desmoplakin  (Proteintech)
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Proteintech desmoplakin
A Schematic of the desmosome under tension. The N-terminal region of DP transitions from a closed conformation to an open conformation. B Representative STED images of DPC (green) <t>and</t> <t>Dsg2</t> (red) at the cell border for WT and K19-KO cells. Scale bar: 500 nm. C Representative STED images of <t>DPN</t> (green) and Dsg2 (red) at the cell border for WT and K19-KO cells. Scale bar: 500 nm. D Quantification of desmosome half-unit widths (Dsg2-DPC distance) from WT and K19-KO cells. n = 1260 (WT), 1010 (K19-KO); N = 3. Two-sided Mann–Whitney’s U test; P = 1.542E–66, *** P < 0.001. The distances between Dsg2 and DPC are significantly greater in the WT compared to the K19-KO cells. E Quantification of desmosome half-unit widths (Dsg2-DPN distance) from WT and K19-KO cells. n = 692 (WT), 826 (K19-KO); N = 3. Two-sided Mann–Whitney’s U test; ns, P > 0.05. The Dsg2-DPN distance is similar in both cell lines. F The mean values from the results in D and E are summarized in the bar chart to compare the DP length (DPN - DPC distance) between the WT and K19-KO cells. The DP length is 66 nm for the WT and 33 nm for the K19-KO, indicating that DP extends 33 nm in the WT cells. G The entire plakin domain structure predicted by AlphaFold2 suggests a U-shape conformation in the absence of force. Two common electrostatic interactions (R592-N744 and K444-E858) observed in all 3 MD simulations (below) are shown. H During the MD simulations, 10 to 15 hydrogen bonds were formed between the plakin domain’s long arm (SR3-4 and SR5-6) and short arm (SR7-8 and SR8-CT). I During the SMD simulations, the distance between the plakin domain’s C-terminus and N-terminus increased by 30~33 nm. This elongation correlates with the distance change experimentally measured in Fig. . J Comparison of the plakin domain structure at the start (left) and at the end (right) of the SMD simulation. The structures show that the plakin domain was elongated by the pulling force without significant secondary structure unfolding. All boxplots show median, 25th and 75th percentile with whiskers reaching the last data point within 1.5× interquartile range. Data points outside this range are plotted individually as outliers. The number of data points n represents the number of line scans across the desmosomes.
Desmoplakin, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/desmoplakin/product/Proteintech
Average 93 stars, based on 1 article reviews
desmoplakin - by Bioz Stars, 2026-05
93/100 stars
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Image Search Results


A Schematic of the desmosome under tension. The N-terminal region of DP transitions from a closed conformation to an open conformation. B Representative STED images of DPC (green) and Dsg2 (red) at the cell border for WT and K19-KO cells. Scale bar: 500 nm. C Representative STED images of DPN (green) and Dsg2 (red) at the cell border for WT and K19-KO cells. Scale bar: 500 nm. D Quantification of desmosome half-unit widths (Dsg2-DPC distance) from WT and K19-KO cells. n = 1260 (WT), 1010 (K19-KO); N = 3. Two-sided Mann–Whitney’s U test; P = 1.542E–66, *** P < 0.001. The distances between Dsg2 and DPC are significantly greater in the WT compared to the K19-KO cells. E Quantification of desmosome half-unit widths (Dsg2-DPN distance) from WT and K19-KO cells. n = 692 (WT), 826 (K19-KO); N = 3. Two-sided Mann–Whitney’s U test; ns, P > 0.05. The Dsg2-DPN distance is similar in both cell lines. F The mean values from the results in D and E are summarized in the bar chart to compare the DP length (DPN - DPC distance) between the WT and K19-KO cells. The DP length is 66 nm for the WT and 33 nm for the K19-KO, indicating that DP extends 33 nm in the WT cells. G The entire plakin domain structure predicted by AlphaFold2 suggests a U-shape conformation in the absence of force. Two common electrostatic interactions (R592-N744 and K444-E858) observed in all 3 MD simulations (below) are shown. H During the MD simulations, 10 to 15 hydrogen bonds were formed between the plakin domain’s long arm (SR3-4 and SR5-6) and short arm (SR7-8 and SR8-CT). I During the SMD simulations, the distance between the plakin domain’s C-terminus and N-terminus increased by 30~33 nm. This elongation correlates with the distance change experimentally measured in Fig. . J Comparison of the plakin domain structure at the start (left) and at the end (right) of the SMD simulation. The structures show that the plakin domain was elongated by the pulling force without significant secondary structure unfolding. All boxplots show median, 25th and 75th percentile with whiskers reaching the last data point within 1.5× interquartile range. Data points outside this range are plotted individually as outliers. The number of data points n represents the number of line scans across the desmosomes.

Journal: Nature Communications

Article Title: Actomyosin forces trigger a conformational change in desmoplakin within desmosomes

doi: 10.1038/s41467-025-64124-4

Figure Lengend Snippet: A Schematic of the desmosome under tension. The N-terminal region of DP transitions from a closed conformation to an open conformation. B Representative STED images of DPC (green) and Dsg2 (red) at the cell border for WT and K19-KO cells. Scale bar: 500 nm. C Representative STED images of DPN (green) and Dsg2 (red) at the cell border for WT and K19-KO cells. Scale bar: 500 nm. D Quantification of desmosome half-unit widths (Dsg2-DPC distance) from WT and K19-KO cells. n = 1260 (WT), 1010 (K19-KO); N = 3. Two-sided Mann–Whitney’s U test; P = 1.542E–66, *** P < 0.001. The distances between Dsg2 and DPC are significantly greater in the WT compared to the K19-KO cells. E Quantification of desmosome half-unit widths (Dsg2-DPN distance) from WT and K19-KO cells. n = 692 (WT), 826 (K19-KO); N = 3. Two-sided Mann–Whitney’s U test; ns, P > 0.05. The Dsg2-DPN distance is similar in both cell lines. F The mean values from the results in D and E are summarized in the bar chart to compare the DP length (DPN - DPC distance) between the WT and K19-KO cells. The DP length is 66 nm for the WT and 33 nm for the K19-KO, indicating that DP extends 33 nm in the WT cells. G The entire plakin domain structure predicted by AlphaFold2 suggests a U-shape conformation in the absence of force. Two common electrostatic interactions (R592-N744 and K444-E858) observed in all 3 MD simulations (below) are shown. H During the MD simulations, 10 to 15 hydrogen bonds were formed between the plakin domain’s long arm (SR3-4 and SR5-6) and short arm (SR7-8 and SR8-CT). I During the SMD simulations, the distance between the plakin domain’s C-terminus and N-terminus increased by 30~33 nm. This elongation correlates with the distance change experimentally measured in Fig. . J Comparison of the plakin domain structure at the start (left) and at the end (right) of the SMD simulation. The structures show that the plakin domain was elongated by the pulling force without significant secondary structure unfolding. All boxplots show median, 25th and 75th percentile with whiskers reaching the last data point within 1.5× interquartile range. Data points outside this range are plotted individually as outliers. The number of data points n represents the number of line scans across the desmosomes.

Article Snippet: The following primary antibodies were used: human anti-Dsg2 (MAB947, R&D systems), rabbit anti-Dsg2 (21880-1-AP, Proteintech), rabbit anti-DPC antibody (A303-356A, Bethyl Lab), rabbit anti-DPN antibody (25318-1-AP, Proteintech), chicken anti-GFP (600-901-215, Rockland), mouse anti-K19 antibody (A53-B/A2, Santa Cruz Biotechnology), mouse anti-K8 antibody (MA1-06318, ThermoFisher), mouse anti-K18 antibody (MA1-19047, ThermoFisher), control mouse IgG (sc-2025, Santa Cruz Biotechnology), and mouse anti-actin antibody (66009-1-Ig, Proteintech).

Techniques: Comparison

A Schematic of polarized CMs. Myofibrils terminate at the axial membrane. The lateral membrane runs parallel to the myofibrils. B Representative STED images of axially aligned desmosomes in CMs. The CMs were treated with DMSO (CM, i) or Blebbistatin (CM+Blebb, ii), and immunolabeled for DPC (red), Dsg2 (yellow), and F-actin (cyan). Scale bar: 3 µm. Insets display characteristic DP “railroad track” patterns at the junction. C Representative STED images of laterally aligned desmosomes in CMs treated with DMSO (CM, i) or Blebbistatin (CM+Blebb, ii). Scale bar: 3 µm. Insets display DP “railroad track” patterns. D Quantification of axially aligned desmosome widths (DPC-DPC distance) in CM and CM+Blebb cells. n = 384 (CM), 330 (CM+Blebb). Two-sided Mann–Whitney’s U test; P = 9.813E–28, *** P < 0.001. E Quantification of laterally aligned desmosome widths (DPC-DPC distance) in CM and CM+Blebb cells. n = 239 (CM), 297 (CM+Blebb). Two-sided Mann–Whitney’s U test; ns, P > 0.05. F Quantification of axially aligned desmosome widths (DPN-DPN distance) in CM and CM+Blebb cells. n = 498 (CM), 476 (CM+Blebb). Two-sided Mann–Whitney’s U test; ns, P > 0.05. G Quantification of laterally aligned desmosome widths (DPN-DPN distance) in CM and CM+Blebb cells. n = 236 (CM), 187 (CM+Blebb). Two-sided Mann–Whitney’s U test; ns, P > 0.05. Desmosomes in ( D – G ) were analyzed from CMs isolated from 20 to 24 pups total from two separate preps. H Model for force-induced DP conformational change in desmosomes. When desmosomes experience no tension, DP adopts a folded (closed) conformation. Under mechanical stress, the flexible DP plakin domain unfolds to an extended (open) conformation. All boxplots show median, 25th and 75th percentile with whiskers reaching the last data point within 1.5× interquartile range. Data points outside this range are plotted individually as outliers. The number of data points n represents the number of line scans across the desmosomes.

Journal: Nature Communications

Article Title: Actomyosin forces trigger a conformational change in desmoplakin within desmosomes

doi: 10.1038/s41467-025-64124-4

Figure Lengend Snippet: A Schematic of polarized CMs. Myofibrils terminate at the axial membrane. The lateral membrane runs parallel to the myofibrils. B Representative STED images of axially aligned desmosomes in CMs. The CMs were treated with DMSO (CM, i) or Blebbistatin (CM+Blebb, ii), and immunolabeled for DPC (red), Dsg2 (yellow), and F-actin (cyan). Scale bar: 3 µm. Insets display characteristic DP “railroad track” patterns at the junction. C Representative STED images of laterally aligned desmosomes in CMs treated with DMSO (CM, i) or Blebbistatin (CM+Blebb, ii). Scale bar: 3 µm. Insets display DP “railroad track” patterns. D Quantification of axially aligned desmosome widths (DPC-DPC distance) in CM and CM+Blebb cells. n = 384 (CM), 330 (CM+Blebb). Two-sided Mann–Whitney’s U test; P = 9.813E–28, *** P < 0.001. E Quantification of laterally aligned desmosome widths (DPC-DPC distance) in CM and CM+Blebb cells. n = 239 (CM), 297 (CM+Blebb). Two-sided Mann–Whitney’s U test; ns, P > 0.05. F Quantification of axially aligned desmosome widths (DPN-DPN distance) in CM and CM+Blebb cells. n = 498 (CM), 476 (CM+Blebb). Two-sided Mann–Whitney’s U test; ns, P > 0.05. G Quantification of laterally aligned desmosome widths (DPN-DPN distance) in CM and CM+Blebb cells. n = 236 (CM), 187 (CM+Blebb). Two-sided Mann–Whitney’s U test; ns, P > 0.05. Desmosomes in ( D – G ) were analyzed from CMs isolated from 20 to 24 pups total from two separate preps. H Model for force-induced DP conformational change in desmosomes. When desmosomes experience no tension, DP adopts a folded (closed) conformation. Under mechanical stress, the flexible DP plakin domain unfolds to an extended (open) conformation. All boxplots show median, 25th and 75th percentile with whiskers reaching the last data point within 1.5× interquartile range. Data points outside this range are plotted individually as outliers. The number of data points n represents the number of line scans across the desmosomes.

Article Snippet: The following primary antibodies were used: human anti-Dsg2 (MAB947, R&D systems), rabbit anti-Dsg2 (21880-1-AP, Proteintech), rabbit anti-DPC antibody (A303-356A, Bethyl Lab), rabbit anti-DPN antibody (25318-1-AP, Proteintech), chicken anti-GFP (600-901-215, Rockland), mouse anti-K19 antibody (A53-B/A2, Santa Cruz Biotechnology), mouse anti-K8 antibody (MA1-06318, ThermoFisher), mouse anti-K18 antibody (MA1-19047, ThermoFisher), control mouse IgG (sc-2025, Santa Cruz Biotechnology), and mouse anti-actin antibody (66009-1-Ig, Proteintech).

Techniques: Membrane, Immunolabeling, Isolation