Skip to Main Content

Advertisement

Skip Nav Destination
Newest Articles
Article | Excitation–Contraction Coupling
Mathilde Chivet, Maximilian McCluskey, Anne Sophie Nicot, Julie Brocard, Mathilde Beaufils, Diane Giovannini, Benoit Giannesini, Brice Poreau, Jacques Brocard, Sandrine Humbert, Frédéric Saudou, Julien Fauré, Isabelle Marty
The Huntingtin protein, well known for its involvement in the neurodegenerative Huntington’s disease, is also expressed in skeletal muscle. The work presented here is dedicated to a better understanding of its function in skeletal muscle through the development and characterization of KO models.
Article
Matvey Pilagov, Laurens W.H.J. Heling, Jonathan Walklate, Michael A. Geeves, Neil M. Kad
Control of muscle contraction is still not understood. Here, we image fluorescently tagged ATP with single-molecule precision to reveal the activity of individual myosins in different sarcomeric locations. We show how treatment with PKA and the FDA-approved drug mavacamten affects relaxed myofibrils.
Article
Savyon Mazgaoker, Ido Weiser-Bitoun, Inbar Brosh, Ofer Binah, Yael Yaniv
The automaticity of human-induced pluripotent stem cell–derived cardiomyocytes is regulated by a coupled-clock system of the Ca2+ and membrane clocks. We found that the coupled-clock system is regulated by local Ca2+ releases and cAMP/PKA-dependent coupling of the Ca2+ clock to the membrane clock.
Article
Vilius Kurauskas, Marco Tonelli, Katherine Henzler-Wildman
The dominant models explaining potassium channel gating often invoke widening and narrowing of the helix bundle crossing. This paper shows that a closely related channel, NaK, is not gated by this mechanism as the helix bundle crossing in the nonconducting channel is already open.
Article
Merouann Kassa, Jonathan Bradley, Abdelali Jalil, Isabel Llano
Optical activation of channel rhodopsin is used to increase neuronal activity. In cerebellar interneurons, it actually leads to a biphasic activation/inhibition sequence. In these cells, activation of KCa1.1 channels contributes to the post-stimulus inhibition.
Methods and Approaches
Takashi Murayama, Nagomi Kurebayashi, Takuro Numaga-Tomita, Takuya Kobayashi, Satoru Okazaki, Kyosuke Yamashiro, Tsutomu Nakada, Shuichi Mori, Ryosuke Ishida, Hiroyuki Kagechika, Mitsuhiko Yamada, Takashi Sakurai
Mutations in essential components for depolarization-induced Ca2+ release (DICR) are implicated into various skeletal muscle diseases. Murayama et al. establish a reconstituted DICR platform in nonmuscle cells for validation of disease-causing mutations and drug discovery.
Article | Mechanotransduction by Membrane Proteins
Shadi Fuladi, Sarah McGuinness, Le Shen, Christopher R. Weber, Fatemeh Khalili-Araghi
Claudins in tight junctions form ion channels that regulate paracellular permeability. We use molecular dynamics simulations of claudin-15 strands formed by up to 300 monomers to uncover the molecular mechanism of strand flexibility.

Related Articles from Rockefeller University Press

Issue Cover
Current Issue
Volume 154,
Issue 11,
7 November 2022
Reviews & Opinions
Commentary | Myofilament Function 2022
Raúl Padrón, Debabrata Dutta, Roger Craig
The two heads of myosin II interact with each other and with the proximal part of the myosin tail, forming the interacting-heads motif (IHM). The IHM is normally thought of as a single, unique structure, but there are several variants, with important energetic and pathophysiological consequences.
Research News
Ben Short
Researchers develop experimental platform that could be used to evaluate mutations and screen drugs for skeletal muscle diseases.
Commentary
Brad S. Rothberg
Previous crystallographic studies depicted a physical gate of the NaK channel localized at a bundle crossing of pore-lining helices, but solution NMR studies in the current issue of JGP suggest otherwise.

Most Read

Advertisement

Tweets by @JGenPhysiol

Special Collections

Special Collections

A special collection highlighting recent articles addressing a wide range of biophysical questions

View Collections

Close Modal

or Create an Account

Close Modal
Close Modal