#apaperaday Yuzu too busy with antics to make confetti from today's pick from Journal of Biological Chemistry by Upadhyay et al on binding of dystrobrevin to dystrophin. Disclaimer: not an expert on this topic. Requested by @debrobins.bsky.social quite some time ago DOI: 10.1016/j.jbc.2024.108002
April 15, 2025 at 6:33 AM
#apaperaday Yuzu too busy with antics to make confetti from today's pick from Journal of Biological Chemistry by Upadhyay et al on binding of dystrobrevin to dystrophin. Disclaimer: not an expert on this topic. Requested by @debrobins.bsky.social quite some time ago DOI: 10.1016/j.jbc.2024.108002
So far, the focus mainly has been on alpha dystrobrevin. Knocking out alpha dystrobrevin in a mouse model leads to mild muscle problems. It would be interesting to also study what happens when beta dystrobrevin is knocked out (anticipate brain problems).
April 15, 2025 at 6:48 AM
So far, the focus mainly has been on alpha dystrobrevin. Knocking out alpha dystrobrevin in a mouse model leads to mild muscle problems. It would be interesting to also study what happens when beta dystrobrevin is knocked out (anticipate brain problems).
Authors discuss that the alpha dystrobrevin is expressed in amongst others muscle, while beta dystrobrevin is expressed in amongst others brain. This is interesting and I think studies into how the binding differs would be interesting, also in the context of brain comorbidity.
April 15, 2025 at 6:45 AM
Authors discuss that the alpha dystrobrevin is expressed in amongst others muscle, while beta dystrobrevin is expressed in amongst others brain. This is interesting and I think studies into how the binding differs would be interesting, also in the context of brain comorbidity.
New Research on Duchenne Muscular Dystrophy Protein Interactions Lead to More Targeted Therapies
Read More: dmdwarrior.com/new-research...
#dmd #duchenne #bmd #becker #genetherapy #dmdwarrior #dmdwarriors #duchennewarriors #duchenne #musculardystrophy #gene #dna #dystrophin #dystrobrevin
Read More: dmdwarrior.com/new-research...
#dmd #duchenne #bmd #becker #genetherapy #dmdwarrior #dmdwarriors #duchennewarriors #duchenne #musculardystrophy #gene #dna #dystrophin #dystrobrevin
January 1, 2025 at 9:51 AM
New Research on Duchenne Muscular Dystrophy Protein Interactions Lead to More Targeted Therapies
Read More: dmdwarrior.com/new-research...
#dmd #duchenne #bmd #becker #genetherapy #dmdwarrior #dmdwarriors #duchennewarriors #duchenne #musculardystrophy #gene #dna #dystrophin #dystrobrevin
Read More: dmdwarrior.com/new-research...
#dmd #duchenne #bmd #becker #genetherapy #dmdwarrior #dmdwarriors #duchennewarriors #duchenne #musculardystrophy #gene #dna #dystrophin #dystrobrevin
Cortactin interacts with αDystrobrevin-1 and regulates neuromuscular junction morphology https://www.biorxiv.org/content/10.1101/2023.10.13.562179v1
Cortactin interacts with αDystrobrevin-1 and regulates neuromuscular junction morphology https://www.biorxiv.org/content/10.1101/2023.10.13.562179v1
Background: Neuromuscular junctions allow for transmitting signals from the nervous system to skelet
www.biorxiv.org
October 17, 2023 at 3:16 PM
Cortactin interacts with αDystrobrevin-1 and regulates neuromuscular junction morphology https://www.biorxiv.org/content/10.1101/2023.10.13.562179v1
Binding partners have been identified and the DGC consists of alpha and beta dystroglycan, 4 sarcoglycans (alpha, beta, gamma, delta), sarcospan, alpha dystrobrevin, syntrophin and of course our favorite protein: dystrophin.
December 20, 2024 at 7:50 AM
Binding partners have been identified and the DGC consists of alpha and beta dystroglycan, 4 sarcoglycans (alpha, beta, gamma, delta), sarcospan, alpha dystrobrevin, syntrophin and of course our favorite protein: dystrophin.
Authors also discuss how their micro-dystrophin differs from other micro-dystrophins that are tested in trials. It has the C-terminal domain, that can bind to dystrobrevin and syntrophin, the latter in turn can recruit nNOS.
May 6, 2026 at 8:11 AM
Authors also discuss how their micro-dystrophin differs from other micro-dystrophins that are tested in trials. It has the C-terminal domain, that can bind to dystrobrevin and syntrophin, the latter in turn can recruit nNOS.
Authors also point out in the discussion that in addition to dystrobrevin, the c-terminal domain also binds to syntrophin (which can recruit nNOS, just like dystrophin can do directly).
April 15, 2025 at 6:49 AM
Authors also point out in the discussion that in addition to dystrobrevin, the c-terminal domain also binds to syntrophin (which can recruit nNOS, just like dystrophin can do directly).
Both microdystrophins were correctly located at the fiber membrane and improved the force of the EDL muscle. The CT+ microdystrophin protected more against a force drop after eccentric exercise. The microdystrophins could recruit syntrophin and alpha dystrobrevin, but +CT did much better👇
November 7, 2025 at 12:22 PM
Both microdystrophins were correctly located at the fiber membrane and improved the force of the EDL muscle. The CT+ microdystrophin protected more against a force drop after eccentric exercise. The microdystrophins could recruit syntrophin and alpha dystrobrevin, but +CT did much better👇
There is a lot of alternative splicing in the C-terminal domain, also involving the binding domains for dystrobrevin and syntrophin. This suggested to researchers creating micro-dystrophin, perhaps the domain was not crucial. However, authors stress that there will be functions.
April 15, 2025 at 6:50 AM
There is a lot of alternative splicing in the C-terminal domain, also involving the binding domains for dystrobrevin and syntrophin. This suggested to researchers creating micro-dystrophin, perhaps the domain was not crucial. However, authors stress that there will be functions.
Note that the full reversibility of proteins after denaturation is not common. Authors then studied the interaction of alpha and beta dystrobrevin with dystrophin, seeing that this happens at the helices of the dystrophin protein and that upon binding, dystrophin forms more coils than without.
April 15, 2025 at 6:42 AM
Note that the full reversibility of proteins after denaturation is not common. Authors then studied the interaction of alpha and beta dystrobrevin with dystrophin, seeing that this happens at the helices of the dystrophin protein and that upon binding, dystrophin forms more coils than without.
Some micro-dystrophins contain only the cysteine rich domain, so they cannot bind to the dystrobrevin and syntrophins and this may destabilize the DGC and reduce its signaling functions. The regenxbio micro-dystrophin DOES contain also the C-terminal domain.
December 20, 2024 at 8:05 AM
Some micro-dystrophins contain only the cysteine rich domain, so they cannot bind to the dystrobrevin and syntrophins and this may destabilize the DGC and reduce its signaling functions. The regenxbio micro-dystrophin DOES contain also the C-terminal domain.
So I agree with the authors that suggests it has a function. Authors here study the interaction between dystrophin and dystrobrevin. They do this by producing protein fragments for the proteins containing the binding domains. Structure predictions suggest the dystrobrevins have helices.
April 15, 2025 at 6:39 AM
So I agree with the authors that suggests it has a function. Authors here study the interaction between dystrophin and dystrobrevin. They do this by producing protein fragments for the proteins containing the binding domains. Structure predictions suggest the dystrobrevins have helices.
However, the C-terminal domain (coded by exon 71-79) is less well studied and thought to be redundant. It is also lacking in most micro-dystrophin (except that of RegenXbio). This domain binds to dystrobrevin however. Furthermore mutations in the C-terminal domain can cause dystrophinopathy.
April 15, 2025 at 6:36 AM
However, the C-terminal domain (coded by exon 71-79) is less well studied and thought to be redundant. It is also lacking in most micro-dystrophin (except that of RegenXbio). This domain binds to dystrobrevin however. Furthermore mutations in the C-terminal domain can cause dystrophinopathy.
I am not sure how physiological relevant this is. In our body the dystrophin protein has more context than only this fragment and it is never present at the high concentrations authors use here. The alpha and beta dystrobrevin proteins were more stable, but denaturation was also fully reversible.
April 15, 2025 at 6:41 AM
I am not sure how physiological relevant this is. In our body the dystrophin protein has more context than only this fragment and it is never present at the high concentrations authors use here. The alpha and beta dystrobrevin proteins were more stable, but denaturation was also fully reversible.
It also clamps beta-dystroglycan to the sarcoglycans. For dystrophin sadly the authors only modelled the last part, containing the cysteine rich and C-terminal domains, which interact directly with beta-dystroglycan (cysteine rich) and alpha dystrobrevin (C-terminal).
December 20, 2024 at 8:03 AM
It also clamps beta-dystroglycan to the sarcoglycans. For dystrophin sadly the authors only modelled the last part, containing the cysteine rich and C-terminal domains, which interact directly with beta-dystroglycan (cysteine rich) and alpha dystrobrevin (C-terminal).
Do you take requests AAR? ...seems to be more molecular investigations to explain unknown phenotypical variation. Pls share your wisdom about these gene/GW linkages and their impact? www.jbc.org/article/S002...
doi.org/10.3389/fgen...
doi.org/10.3389/fgen...
Biophysical characterization of the dystrophin C-terminal domain: Dystrophin interacts differentially with dystrobrevin isoforms
Duchenne muscular dystrophy (DMD) gene encodes dystrophin, a large multidomain protein.
Its nonfunctionality leads to dystrophinopathies like DMD and Becker muscular dystrophy,
for which no cure is ye...
www.jbc.org
February 19, 2025 at 2:20 AM
Do you take requests AAR? ...seems to be more molecular investigations to explain unknown phenotypical variation. Pls share your wisdom about these gene/GW linkages and their impact? www.jbc.org/article/S002...
doi.org/10.3389/fgen...
doi.org/10.3389/fgen...
A groundbreaking study has shed light on the complex interactions between dystrophin, a protein critical to muscle stability, and its partner protein, dystrobrevin, offering new pathways for understanding and treating Duchenne Muscular Dystrophy (DMD).
Published
skylinenews.world/2025/01/01/n...
Published
skylinenews.world/2025/01/01/n...
New study uncovers key insights into protein interactions in Duchenne muscular dystrophy, paving way for more targeted therapies
A groundbreaking study has shed light on the complex interactions between dystrophin, a protein critical to muscle stability, and its partner protein, dystrobrevin, offering new pathways for understanding and treating Duchenne Muscular Dystrophy (DMD). Published in the December issue of the Journal of Biological Chemistry, researchers characterize the mysterious C-terminal (CT) domain of dystrophin and […]
skylinenews.world
January 1, 2025 at 1:57 PM
A groundbreaking study has shed light on the complex interactions between dystrophin, a protein critical to muscle stability, and its partner protein, dystrobrevin, offering new pathways for understanding and treating Duchenne Muscular Dystrophy (DMD).
Published
skylinenews.world/2025/01/01/n...
Published
skylinenews.world/2025/01/01/n...
New insights into protein roles in Duchenne muscular dystrophy
Credit: Journal of Biological Chemistry (2024). DOI: 10.1016/j.jbc.2024.108002 A new study has shed light on the complex interactions between dystrophin, a protein critical to muscle stability, and its partner protein, dystrobrevin,…
Credit: Journal of Biological Chemistry (2024). DOI: 10.1016/j.jbc.2024.108002 A new study has shed light on the complex interactions between dystrophin, a protein critical to muscle stability, and its partner protein, dystrobrevin,…
New insights into protein roles in Duchenne muscular dystrophy
Credit: Journal of Biological Chemistry (2024). DOI: 10.1016/j.jbc.2024.108002 A new study has shed light on the complex interactions between dystrophin, a protein critical to muscle stability, and its partner protein, dystrobrevin, offering new pathways for understanding and treating Duchenne Muscular Dystrophy (DMD). Published in the December issue of the Journal of Biological Chemistry, researchers characterize the mysterious C-terminal (CT) domain of dystrophin and its role in stabilizing cellular membranes across various tissues.
todayheadline.co
January 2, 2025 at 9:13 AM
New insights into protein roles in Duchenne muscular dystrophy
Credit: Journal of Biological Chemistry (2024). DOI: 10.1016/j.jbc.2024.108002 A new study has shed light on the complex interactions between dystrophin, a protein critical to muscle stability, and its partner protein, dystrobrevin,…
Credit: Journal of Biological Chemistry (2024). DOI: 10.1016/j.jbc.2024.108002 A new study has shed light on the complex interactions between dystrophin, a protein critical to muscle stability, and its partner protein, dystrobrevin,…
A recent study uncovers the complex interactions between dystrophin and dystrobrevin, paving the way for new Duchenne Muscular Dystrophy treatments.
New Insights into Dystrophin-Dystrobrevin Interactions Could Revolutionize Duchenne Muscular Dystrophy Treatments
A recent study uncovers the complex interactions between dystrophin and dystrobrevin, paving the way for new Duchenne Muscular Dystrophy treatments.
www.science-tldr.com
January 2, 2025 at 8:30 AM
A recent study uncovers the complex interactions between dystrophin and dystrobrevin, paving the way for new Duchenne Muscular Dystrophy treatments.
Cortactin interacts with αDystrobrevin-1 and regulates neuromuscular junction morphology https://www.biorxiv.org/content/10.1101/2023.10.13.562179v1
Cortactin interacts with αDystrobrevin-1 and regulates neuromuscular junction morphology https://www.biorxiv.org/content/10.1101/2023.10.13.562179v1
Background: Neuromuscular junctions allow for transmitting signals from the nervous system to skelet
www.biorxiv.org
October 17, 2023 at 3:16 PM
Cortactin interacts with αDystrobrevin-1 and regulates neuromuscular junction morphology https://www.biorxiv.org/content/10.1101/2023.10.13.562179v1