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Special Issue "Ca2+-Activated Chloride Channels and Phospholipid Scramblases"

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: 31 March 2021.

Special Issue Editors

Dr. Anna Boccaccio

Guest Editor
Institute of Biophysics, National Research Council, I-16149 Genova, Italy
Interests: ion channels; scramblases; membrane biophysics; electrophysiology; Ca-activated chloride channels; TMEM16; volume-regulated chloride channels; molecular and cellular mechanisms of genetic diseases; olfaction; olfactory transduction; channelopathies; intracellular channels
Dr. Simone Pifferi

Guest Editor
Department of Experimental and Clinical Medicine, Università Politecnica delle Marche, I-60126 Ancona, Italy
Interests: ion channels; scramblases; membrane biophysics; electrophysiology; Ca-activated chloride channels; TMEM16; olfaction; olfactory transduction; vomeronsal trasnduction

Special Issue Information

Dear Colleagues,

TMEM16A/Ano1 and TMEM16B/Ano2 form Ca2+-activated Cl channels that are involved in a variety of physiological functions, such as transepithelial ion transport, olfaction, phototransduction, smooth muscle contraction, nociception, cell proliferation and neuronal excitability.

Ca2+-activated Cl currents were first observed in the early 1980s in the salamander retina and in Xenopus laevis oocytes, however the lack of knowledge on their molecular identity and poor pharmacological tools has slowed the comprehension of their specific physiological functions for a long time. Additionally, a full comprehension of their function cannot neglect the equilibrium potential for chloride. In the central and peripheral nervous systems, a contribution of these currents to cellular excitability has been proposed, either excitatory, as in dorsal root ganglion neurons and olfactory sensory neurons, or inhibitory, as in thalamocortical neurons.

Surprisingly, despite sharing a similar structural organization, other members of the TMEM16/Anoctamin family have a completely different molecular function: these so-called Ca2+ dependent phospholipid scramblases mediate the passive transfer of phospholipids between the leaflets of the membrane bilayer, causing the regulated collapse of membrane asymmetry.

While the TMEM16F/Ano6 scramblase resides in the plasma membrane, others, including TMEM16E/Ano5 and TMEM16K/Ano10 may function in intracellular membranes. Mutations in several TMEM16/Anoctamin genes, TMEM16C/Ano3, TMEM16E/Ano5, TMEM16F/Ano6 and TMEM16K/Ano10, cause various genetic diseases, however their molecular physio-pathology is not established yet.

Following the recent progress on this unique protein family and with new techniques becoming available, these are exciting times to study all aspects of TMEM16 physiology.

This Special Issue calls for original research, full reviews, and perspectives that address the current knowledge in the  field  of Ca2+-activated chloride channels and scramblases.

Dr. Anna Boccaccio
Dr. Simone Pifferi

Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • Ion channels
  • molecular mechanisms
  • genetic disease
  • Ca2+-activated chloride channels
  • Phospholipid scramblase
  • TMEM16
  • Anoctamin
  • Chloride
  • Ca2+-activated channels
  • PtdSer
  • electrophysiology
  • membrane asymmetry

Published Papers (1 paper)

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Research

Open AccessArticle
Divalent Cation Modulation of Ion Permeation in TMEM16 Proteins
Int. J. Mol. Sci. 2021, 22(4), 2209; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms22042209 - 23 Feb 2021
Abstract
Intracellular divalent cations control the molecular function of transmembrane protein 16 (TMEM16) family members. Both anion channels (such as TMEM16A) and phospholipid scramblases (such as TMEM16F) in this family are activated by intracellular Ca2+ in the low µM range. In addition, intracellular [...] Read more.
Intracellular divalent cations control the molecular function of transmembrane protein 16 (TMEM16) family members. Both anion channels (such as TMEM16A) and phospholipid scramblases (such as TMEM16F) in this family are activated by intracellular Ca2+ in the low µM range. In addition, intracellular Ca2+ or Co2+ at mM concentrations have been shown to further potentiate the saturated Ca2+-activated current of TMEM16A. In this study, we found that all alkaline earth divalent cations in mM concentrations can generate similar potentiation effects in TMEM16A when applied intracellularly, and that manipulations thought to deplete membrane phospholipids weaken the effect. In comparison, mM concentrations of divalent cations minimally potentiate the current of TMEM16F but significantly change its cation/anion selectivity. We suggest that divalent cations may increase local concentrations of permeant ions via a change in pore electrostatic potential, possibly acting through phospholipid head groups in or near the pore. Monovalent cations appear to exert a similar effect, although with a much lower affinity. Our findings resolve controversies regarding the ion selectivity of TMEM16 proteins. The physiological role of this mechanism, however, remains elusive because of the nearly constant high cation concentrations in cytosols. Full article
(This article belongs to the Special Issue Ca2+-Activated Chloride Channels and Phospholipid Scramblases)
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