Skip to Main Content


Skip Nav Destination
Newest Articles
Chiara Stronczek, Stephan Lange, Belinda Bullard, Sebastian Wolniak, Emma Börgeson, Olga Mayans, Jennifer R. Fleming
Stronczek et al. analyze the structure of the titin-N2A poly-Ig segment, a key signaling element in the sarcomere. They reveal a unique topography for the I81-I83 tandem, but they could not confirm the presence of Ca2+ binding sites in I81-I83 or the interaction of N2A with actin.
Mohammad-Reza Ghovanloo, Koushik Choudhury, Tagore S. Bandaru, Mohamed A. Fouda, Kaveh Rayani, Radda Rusinova, Tejas Phaterpekar, Karen Nelkenbrecher, Abeline R. Watkins, Damon Poburko, Jenifer Thewalt, Olaf S. Andersen, Lucie Delemotte, Samuel J. Goodchild, Peter C. Ruben
Ghovanloo et al. combined in silico and in vitro approaches to determine the mechanism by which CBD inhibits the skeletal muscle Na+ channel Nav1.4. Their findings suggest that CBD acts directly, by binding inside the Nav1.4 pore, as well as indirectly, by modulating membrane elasticity.
Leticia G. Marmolejo-Murillo, Iván A. Aréchiga-Figueroa, Eloy G. Moreno-Galindo, Tania Ferrer, Rodrigo Zamora-Cárdenas, Ricardo A. Navarro-Polanco, José A. Sánchez-Chapula, Aldo A. Rodríguez-Menchaca
Inward rectification of Kir channels is attributed to a voltage-dependent block of the channel pore by intracellular cations. Marmolejo-Murillo et al. identify a new intrinsic gating mechanism powered by the K+-flux in Kir4.1/Kir5.1 channels, which induces voltage-dependent inward rectification.
Marcos Matamoros, Colin G. Nichols
Matamoros and Nichols show that mutations in a transmembrane domain outside of the selectivity filter of the KirBac1.1 K+ channel affect ion transport, suggesting that channel selectivity is determined by the physical interaction between different domains.
Chung-Wei Chiang, Wen-Chi Shu, Jun Wan, Beth A. Weaver, Meyer B. Jackson
Chiang et al. recorded spontaneous miniature excitatory postsynaptic currents in cocultures of neurons and HEK cells. They show that this system allows the resolution of the distinct contributions of vesicles, fusion pores, dendrites, and receptors to the dynamic control of synaptic transmission.
Andrew K. Coleman, Humberto C. Joca, Guoli Shi, W. Jonathan Lederer, Christopher W. Ward
Posttranslational modifications in microtubules affect cytoskeletal mechanics and mechanotransduction. In this study, Coleman et al. show that acetylated α-tubulin affects cytoskeletal stiffness and viscoelastic resistance, thus revealing another regulator of striated muscle mechanotransduction.
Bogdan I. Iaparov, Ivan Zahradnik, Alexander S. Moskvin, Alexandra Zahradníková
Iaparov et al. use in silico modeling to test the effect of changes in the geometric arrangement of RYR channels on calcium release in cardiac myocytes. Their simulations predict a coupling between RYR distribution at the calcium release site and dyad function.

Related Articles from Rockefeller University Press

Issue Cover
Current Issue
Volume 153,
Issue 4,
April 5, 2021
Reviews & Opinions
Carsten Mim, Guy Perkins, Gerhard Dahl
Mim et al. discuss discrepancies between the known functions of pannexin 1 as an ATP and chloride channel and recently published cryo-EM structural data, which so far appear consistent only with the chloride channel function.
Emilio Carbone
Using Nav1.3 and FGF14 KO mice, Martinez-Espinosa et al. provide new findings on how intracellular FGF14 proteins interfere with the endogenous fast inactivation gating and regulate the “long-term inactivation” of Nav1.3 channels that sets Nav channel availability and spike adaptation during sustained stimulation in adrenal chromaffin cells.
Christopher Solís, R. John Solaro
This review focuses on thin filament regulatory mechanisms with emphasis on cardiac-specific mechanisms in the three-state model of sarcomere activation and on signaling cascades at the barbed and pointed ends.

Most Read


Tweets by @JGenPhysiol

Special Collections

Special Collections

A special collection of reviews curated from recent issues of JGP

View Collections
Close Modal

or Create an Account

Close Modal
Close Modal