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Omecamtiv mecarbil and Mavacamten target the same myosin pocket despite opposite effects in heart contraction

Omecamtiv mecarbil and Mavacamten are small molecules directly modulating the force produced by β-cardiac myosin. In this work, the authors describe how the modulators Omecamtiv mecarbil and Mavacamten can have opposite effects on cardiac myosin force production despite occupying the same pocket.

Daniel Auguin
Julien Robert-Paganin
Anne Houdusse
ResearchOpen Access07 Jun 2024
Nature Communications

Volume: 15, P: 1-14
Cryo-EM structure of the folded-back state of human β-cardiac myosin

The authors report the high-resolution structure of human β-cardiac myosin in its sequestered state. The results provide insights into the cardiac regulation and represent a tool to investigate the development of inherited cardiomyopathies.

Alessandro Grinzato
Daniel Auguin
Julien Robert-Paganin
ResearchOpen Access31 May 2023
Nature Communications

Volume: 14, P: 1-12
Hypertrophic cardiomyopathy disease results from disparate impairments of cardiac myosin function and auto-inhibition

Hypertrophic cardiomyopathy (HCM) is caused by point mutations in sarcomeric proteins. Here the authors develop an optimized model of the sequestered state of cardiac myosin and define the features affecting the lever arm compliance, allowing them to group mutations in classes and to elucidate the molecular mechanisms leading to cardiac dysfunction in HCM.

Julien Robert-Paganin
Daniel Auguin
Anne Houdusse
ResearchOpen Access01 Oct 2018
Nature Communications

Volume: 9, P: 1-13
Mechanism of small molecule inhibition of Plasmodium falciparum myosin A informs antimalarial drug design

Myosin A (PfMyoA) is essential for the pathogenesis of Plasmodium falciparum, the causative agent of malaria. Here we decipher the mechanism by which a small molecule inhibitor (KNX-002) of PfMyoA impedes its motor activity.

Dihia Moussaoui
James P. Robblee
Anne Houdusse
ResearchOpen Access12 Jun 2023
Nature Communications

Volume: 14, P: 1-12
The actomyosin interface contains an evolutionary conserved core and an ancillary interface involved in specificity

Plasmodium falciparum moves by an atypical process called gliding motility which comprises of atypical myosin A (PfMyoA) and filaments of the dynamic and divergent PfActin-1 (PfAct1). Here authors present the cryo-EM structure of PfMyoA bound to filamentous PfAct1 stabilized with jasplakinolide and provide insights into the interactions that are required for the parasite to produce the force and motion required for infectivity.

Julien Robert-Paganin
Xiao-Ping Xu
Dorit Hanein
ResearchOpen Access25 Mar 2021
Nature Communications

Volume: 12, P: 1-11
Plasmodium myosin A drives parasite invasion by an atypical force generating mechanism

Here, Robert-Paganin et al. show that myosin A from Plasmodium falciparum is critical for red blood cell invasion and that non-canonical interactions and regulated phosphorylation are important for force generation during parasite invasion.

Julien Robert-Paganin
James P. Robblee
Anne Houdusse
ResearchOpen Access23 Jul 2019
Nature Communications

Volume: 10, P: 1-12
A transgenic mouse model for mammary carcinogenesis

Baolin Li
Kristen L Murphy
Jeffrey M Rosen
Research05 Mar 1998
Oncogene

Volume: 16, P: 997-1007
Expression of a p53 mutant in the epidermis of transgenic mice accelerates chemical carcinogenesis

Xiao-Jing Wang
David A Greenhalgh
Dennis R Roop
Research14 Jul 1998
Oncogene

Volume: 17, P: 35-45

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Omecamtiv mecarbil and Mavacamten target the same myosin pocket despite opposite effects in heart contraction

Cryo-EM structure of the folded-back state of human β-cardiac myosin

Hypertrophic cardiomyopathy disease results from disparate impairments of cardiac myosin function and auto-inhibition

Mechanism of small molecule inhibition of Plasmodium falciparum myosin A informs antimalarial drug design

The actomyosin interface contains an evolutionary conserved core and an ancillary interface involved in specificity

Plasmodium myosin A drives parasite invasion by an atypical force generating mechanism

A transgenic mouse model for mammary carcinogenesis

Expression of a p53 mutant in the epidermis of transgenic mice accelerates chemical carcinogenesis

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