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Methods and Approaches
Pablo S. Gaete, Mauricio A. Lillo, William López, Yu Liu, Wenjuan Jiang, Yun Luo, Andrew L. Harris, Jorge E. Contreras
Gaete et al. have designed a methodology that allows quantitative analysis of the permeation of ions and molecules through connexin and CALHM1 large-pore channels. Both channels display saturable transport of molecules that could be described by Michaelis-Menten kinetics with apparent Km and Vmax.
Martin Loynaz Prieto, Kamyar Firouzi, Butrus T. Khuri-Yakub, Daniel V. Madison, Merritt Maduke
Prieto et al. describe how ultrasound can either inhibit or potentiate action potential firing in hippocampal pyramidal neurons and demonstrate that these effects can be explained by increased potassium conductance.
Alejandra Cely-Ortiz, Juan I. Felice, Leandro A. Díaz-Zegarra, Carlos A. Valverde, Marilén Federico, Julieta Palomeque, Xander H.T. Wehrens, Evangelia G. Kranias, Ernesto A. Aiello, Elena C. Lascano, Jorge A. Negroni, Alicia Mattiazzi
The present work shows that SR Ca2+ load and RYR2 Ca2+ sensitivity are major determinants of Ca2+ release restitution (CRR) after each heartbeat. Mathematical modeling led us to speculate that the velocity of SR Ca2+ refilling might regulate CRR independently of SR Ca2+ content.
Vladimir V. Cherny, Boris Musset, Deri Morgan, Sarah Thomas, Susan M.E. Smith, Thomas E. DeCoursey
The voltage-gated proton channel (HV1) resembles the voltage sensors of other channels, but its movement during channel opening remains controversial. Cherny et al. establish open and closed gating configurations of HV1 by analyzing the interactions of Zn2+ with an introduced histidine residue.
Jiali Wang, Kaiqi Zhang, Puja Goyal, Christof Grewer
K+ binding to mammalian glutamate transporters is essential for the import and release of glutamate into cells. Using MD simulations and site-directed mutagenesis, Wang et al. identify two K+ binding sites in the transporter EAAC1, one of which appears to catalyze the relocation step of the transport cycle.
Maria A. Neginskaya, Jasiel O. Strubbe, Giuseppe F. Amodeo, Benjamin A. West, Shoshana Yakar, Jason N. Bazil, Evgeny V. Pavlov
Stress increases the permeability of the mitochondrial inner membrane by activating permeability transition pores (PTPs), likely composed of ATP synthase or the adenine nucleotide translocator. By measuring water flux during calcium-activated mitochondrial swelling, Neginskaya et al. estimate that if these proteins are involved in PTP, only a small fraction becomes transformed into the pore on a single mitochondrion.
Antonio Michelucci, Simona Boncompagni, Laura Pietrangelo, Takahiro Takano, Feliciano Protasi, Robert T. Dirksen
Mice lacking calsequestrin-1 have reduced levels of releasable Ca2+ in the sarcoplasmic reticulum of their skeletal muscles. Michelucci et al. reveal that this is compensated by constitutive assembly of STIM1 and Orai1 into Ca2+ entry units, promoting both constitutive and store-operated Ca2+ entry.

Related Articles from Rockefeller University Press

Current Issue
Volume 152,
Issue 10,
October 5, 2020
Reviews & Opinions
Research News
Ben Short
JGP study describes a novel quantitative assay combining fluorescence microscopy and electrophysiology, which reveals that transport of small molecules through CALHM1 and connexin channels is saturable
Gyorgy Csordas, Stephen Hurst
Neginskaya et al. discuss the very low number of calcium-induced permeability transition pores in the single mitochondrion.
Jasmine A. Nirody, Itay Budin, Padmini Rangamani
This review outlines a holistic framework for studying ATP synthase and emphasizes the importance of considering interactions with the lipid environment in shaping the function and evolutionary history of membrane proteins.

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