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Calmodulin Binding Proteins
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Calmodulin Binding Proteins

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Pathology, Diagnostics, and Therapeutics".

Deadline for manuscript submissions: closed (31 July 2021) | Viewed by 14184

Special Issue Editors

Prof. Dr. Danton O'Day

E-Mail Website
Guest Editor
1. Department of Biology, University of Toronto Mississauga, Mississauga, ON L5L 1C6, Canada
2. Department of Cell and Systems Biology, University of Toronto, Toronto, ON M5S 3G5, Canada
Dr. Robert J. Huber

E-Mail Website
Guest Editor
Department of Biology, Trent University, Peterborough, ON K9L 0G2, Canada
Interests: Dictyostelium discoideum; batten disease (neuronal ceroid lipofuscinosis); signal transduction; protein secretion; extracellular matrix; calcium and calmodulin; cyclin-dependent kinases

Special Issue Information

Dear Colleagues,

Hundreds of different proteins bind to and are regulated by the small calcium-binding protein calmodulin (CaM). These calmodulin binding proteins (CaMBPs) serve multiple, critical biomedical functions. Unlike other protein-protein interactions, binding to CaM does not involve a defined amino acid sequence. Instead, it is mediated by a diversity of canonical and non-canonical calcium-dependent binding motifs and a smaller but still variable number of calcium-independent IQ, IQ-like and other binding domains. Despite this variability, CaMBP regulation is tightly controlled and these proteins mediate diverse cellular functions as enzymes, tethers, adaptors, translocators, ion channels, and regulators of calcium signal transduction. As a result, CaMBPs are critical to a multitude of central biological processes, from inflammation to learning, and memory, as well as to a diversity of diseases including Alzheimer’s, cancers and cardiac arrythmias, to name a few. This comprehensive Special Issue “Calmodulin Binding Proteins” brings the complexity of these topics to light, serving not only as an introduction but also as a guide for future research.

Prof. Dr. Danton O'Day
Dr. Robert J. Huber
Guest Editors

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 submissions that pass pre-check are 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

  • adaptor proteins
  • calcineurin
  • calmodulin binding domains
  • calmodulin-dependent kinases
  • cancer
  • ion channels
  • IQ motifs
  • neurodegeneration
  • protein targeting
  • protein translocation

Published Papers (4 papers)

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Research

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17 pages, 5994 KiB  
Article
A Proteomics Analysis of Calmodulin-Binding Proteins in Dictyostelium discoideum during the Transition from Unicellular Growth to Multicellular Development
by William D. Kim, Shyong Q. Yap and Robert J. Huber
Int. J. Mol. Sci. 2021, 22(4), 1722; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms22041722 - 09 Feb 2021
Viewed by 2339
Abstract
Calmodulin (CaM) is an essential calcium-binding protein within eukaryotes. CaM binds to calmodulin-binding proteins (CaMBPs) and influences a variety of cellular and developmental processes. In this study, we used immunoprecipitation coupled with mass spectrometry (LC-MS/MS) to reveal over 500 putative CaM interactors in [...] Read more.
Calmodulin (CaM) is an essential calcium-binding protein within eukaryotes. CaM binds to calmodulin-binding proteins (CaMBPs) and influences a variety of cellular and developmental processes. In this study, we used immunoprecipitation coupled with mass spectrometry (LC-MS/MS) to reveal over 500 putative CaM interactors in the model organism Dictyostelium discoideum. Our analysis revealed several known CaMBPs in Dictyostelium and mammalian cells (e.g., myosin, calcineurin), as well as many novel interactors (e.g., cathepsin D). Gene ontology (GO) term enrichment and Search Tool for the Retrieval of Interacting proteins (STRING) analyses linked the CaM interactors to several cellular and developmental processes in Dictyostelium including cytokinesis, gene expression, endocytosis, and metabolism. The primary localizations of the CaM interactors include the nucleus, ribosomes, vesicles, mitochondria, cytoskeleton, and extracellular space. These findings are not only consistent with previous work on CaM and CaMBPs in Dictyostelium, but they also provide new insight on their diverse cellular and developmental roles in this model organism. In total, this study provides the first in vivo catalogue of putative CaM interactors in Dictyostelium and sheds additional light on the essential roles of CaM and CaMBPs in eukaryotes. Full article
(This article belongs to the Special Issue Calmodulin Binding Proteins)
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Review

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27 pages, 20966 KiB  
Review
Calmodulin-Connexin Partnership in Gap Junction Channel Regulation-Calmodulin-Cork Gating Model
by Camillo Peracchia and Lillian Mae Leverone Peracchia
Int. J. Mol. Sci. 2021, 22(23), 13055; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms222313055 - 02 Dec 2021
Cited by 5 | Viewed by 2252
Abstract
In the past four decades numerous findings have indicated that gap junction channel gating is mediated by intracellular calcium concentrations ([Ca2+i]) in the high nanomolar range via calmodulin (CaM). We have proposed a CaM-based gating model based on evidence for [...] Read more.
In the past four decades numerous findings have indicated that gap junction channel gating is mediated by intracellular calcium concentrations ([Ca2+i]) in the high nanomolar range via calmodulin (CaM). We have proposed a CaM-based gating model based on evidence for a direct CaM role in gating. This model is based on the following: CaM inhibitors and the inhibition of CaM expression to prevent chemical gating. A CaM mutant with higher Ca2+ sensitivity greatly increases gating sensitivity. CaM co-localizes with connexins. Connexins have high-affinity CaM-binding sites. Connexin mutants paired to wild type connexins have a higher gating sensitivity, which is eliminated by the inhibition of CaM expression. Repeated trans-junctional voltage (Vj) pulses progressively close channels by the chemical/slow gate (CaM’s N-lobe). At the single channel level, the gate closes and opens slowly with on-off fluctuations. Internally perfused crayfish axons lose gating competency but recover it by the addition of Ca-CaM to the internal perfusion solution. X-ray diffraction data demonstrate that isolated gap junctions are gated at the cytoplasmic end by a particle of the size of a CaM lobe. We have proposed two types of CaM-driven gating: “Ca-CaM-Cork” and “CaM-Cork”. In the first, the gating involves Ca2+-induced CaM activation. In the second, the gating occurs without a [Ca2+]i rise. Full article
(This article belongs to the Special Issue Calmodulin Binding Proteins)
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17 pages, 2177 KiB  
Review
Calmodulin Interactions with Voltage-Gated Sodium Channels
by Xin Wu and Liang Hong
Int. J. Mol. Sci. 2021, 22(18), 9798; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms22189798 - 10 Sep 2021
Cited by 13 | Viewed by 3856
Abstract
Calmodulin (CaM) is a small protein that acts as a ubiquitous signal transducer and regulates neuronal plasticity, muscle contraction, and immune response. It interacts with ion channels and plays regulatory roles in cellular electrophysiology. CaM modulates the voltage-gated sodium channel gating process, alters [...] Read more.
Calmodulin (CaM) is a small protein that acts as a ubiquitous signal transducer and regulates neuronal plasticity, muscle contraction, and immune response. It interacts with ion channels and plays regulatory roles in cellular electrophysiology. CaM modulates the voltage-gated sodium channel gating process, alters sodium current density, and regulates sodium channel protein trafficking and expression. Many mutations in the CaM-binding IQ domain give rise to diseases including epilepsy, autism, and arrhythmias by interfering with CaM interaction with the channel. In the present review, we discuss CaM interactions with the voltage-gated sodium channel and modulators involved in CaM regulation, as well as summarize CaM-binding IQ domain mutations associated with human diseases in the voltage-gated sodium channel family. Full article
(This article belongs to the Special Issue Calmodulin Binding Proteins)
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16 pages, 1894 KiB  
Review
Calmodulin Binding Proteins and Alzheimer’s Disease: Biomarkers, Regulatory Enzymes and Receptors That Are Regulated by Calmodulin
by Danton H. O’Day
Int. J. Mol. Sci. 2020, 21(19), 7344; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms21197344 - 05 Oct 2020
Cited by 30 | Viewed by 4623
Abstract
The integral role of calmodulin in the amyloid pathway and neurofibrillary tangle formation in Alzheimer’s disease was first established leading to the “Calmodulin Hypothesis”. Continued research has extended our insight into the central function of the small calcium sensor and effector calmodulin and [...] Read more.
The integral role of calmodulin in the amyloid pathway and neurofibrillary tangle formation in Alzheimer’s disease was first established leading to the “Calmodulin Hypothesis”. Continued research has extended our insight into the central function of the small calcium sensor and effector calmodulin and its target proteins in a multitude of other events associated with the onset and progression of this devastating neurodegenerative disease. Calmodulin’s involvement in the contrasting roles of calcium/CaM-dependent kinase II (CaMKII) and calcineurin (CaN) in long term potentiation and depression, respectively, and memory impairment and neurodegeneration are updated. The functions of the proposed neuronal biomarker neurogranin, a calmodulin binding protein also involved in long term potentiation and depression, is detailed. In addition, new discoveries into calmodulin’s role in regulating glutamate receptors (mGluR, NMDAR) are overviewed. The interplay between calmodulin and amyloid beta in the regulation of PMCA and ryanodine receptors are prime examples of how the buildup of classic biomarkers can underly the signs and symptoms of Alzheimer’s. The role of calmodulin in the function of stromal interaction molecule 2 (STIM2) and adenosine A2A receptor, two other proteins linked to neurodegenerative events, is discussed. Prior to concluding, an analysis of how targeting calmodulin and its binding proteins are viable routes for Alzheimer’s therapy is presented. In total, calmodulin and its binding proteins are further revealed to be central to the onset and progression of Alzheimer’s disease. Full article
(This article belongs to the Special Issue Calmodulin Binding Proteins)
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