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Calmodulin Function in Health and Disease 2.0
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Calmodulin Function in Health and Disease 2.0

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

Deadline for manuscript submissions: closed (31 December 2020) | Viewed by 15220

Special Issue Editors

Prof. Dr. Antonio Villalobo

E-Mail Website1 Website2
Guest Editor
Instituto de Investigaciones Sanitarias (IdiPAZ), Hospital Universitario La Paz, Madrid, Spain
Interests: calcium; calmodulin; cancer; receptor tyrosine kinases EGFR/ErbB1/HER1 and ErbB2/HER2; adaptor protein Grb7; and non-receptor tyrosine kinase Src
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. Martin W. Berchtold

E-Mail Website
Guest Editor
Department of Biology, University of Copenhagen, Copenhagen, Denmark
Interests: cell signaling; cell cycle; cell proliferation; plasma membrane repair; cancer; calcium binding proteins; calmodulin; ALG-2
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Calmodulin is the major intracellular transducer of the Ca2+ signal in all eukaryotic cells, regulating a myriad of cellular processes by modulating the activity of hundreds of proteins, including enzymes, ion channels, transcription factors, receptors for different ligands, adaptors and structural proteins. The multifunctional role of this highly conserved protein is facilitated by its capacity to utilise different occupancy of its four Ca2+-binding sites with distinct affinities and binding kinetics, and its enormous structural flexibility. This allows for simultaneous linkage to distinct or identical proteins and/or two segments of the same protein, forming dimeric complexes or operational motifs with specific functional roles. Post-translational modifications of calmodulin, particularly its phosphorylation, add an additional layer of complexity to the functionality of calmodulin, allowing for drastic modification or subtle modulation of its multiple regulatory roles. In recent years, the discovery of calmodulin mutations in humans has uncovered its critical role in cardiac physiology and enabled new insights into the cause of different types of cardiac arrhythmias. These genetic alterations could be the cause of yet uncovered pathologies. It is expected that the study of calmodulin functionality in health and its dysfunction in disorders, including cancer, could help to identify new potential pharmacological targets to combat different diseases.

Prof. Dr. Antonio Villalobo
Prof. Dr. Martin W. Berchtold
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

  • Ca2+-dependent calmodulin functions
  • Ca2+-independent calmodulin functions
  • Posttranslational calmodulin modifications
  • Calmodulin genetics
  • Calmodulin mutations
  • Calmodulin as adaptor
  • Calmodulin-based Ca2+ sensors
  • Calmodulin inhibitors
  • Calmodulin biophysics
  • Calmodulin in health and disease
  • Calmodulin evolution

Published Papers (4 papers)

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Review

15 pages, 991 KiB  
Review
Calmodulin and Its Binding Proteins in Parkinson’s Disease
by Anastasiia Bohush, Wiesława Leśniak, Serge Weis and Anna Filipek
Int. J. Mol. Sci. 2021, 22(6), 3016; https://doi.org/10.3390/ijms22063016 - 16 Mar 2021
Cited by 16 | Viewed by 2800
Abstract
Parkinson’s disease (PD) is a neurodegenerative disorder that manifests with rest tremor, muscle rigidity and movement disturbances. At the microscopic level it is characterized by formation of specific intraneuronal inclusions, called Lewy bodies (LBs), and by a progressive loss of dopaminergic neurons in [...] Read more.
Parkinson’s disease (PD) is a neurodegenerative disorder that manifests with rest tremor, muscle rigidity and movement disturbances. At the microscopic level it is characterized by formation of specific intraneuronal inclusions, called Lewy bodies (LBs), and by a progressive loss of dopaminergic neurons in the striatum and substantia nigra. All living cells, among them neurons, rely on Ca2+ as a universal carrier of extracellular and intracellular signals that can initiate and control various cellular processes. Disturbances in Ca2+ homeostasis and dysfunction of Ca2+ signaling pathways may have serious consequences on cells and even result in cell death. Dopaminergic neurons are particularly sensitive to any changes in intracellular Ca2+ level. The best known and studied Ca2+ sensor in eukaryotic cells is calmodulin. Calmodulin binds Ca2+ with high affinity and regulates the activity of a plethora of proteins. In the brain, calmodulin and its binding proteins play a crucial role in regulation of the activity of synaptic proteins and in the maintenance of neuronal plasticity. Thus, any changes in activity of these proteins might be linked to the development and progression of neurodegenerative disorders including PD. This review aims to summarize published results regarding the role of calmodulin and its binding proteins in pathology and pathogenesis of PD. Full article
(This article belongs to the Special Issue Calmodulin Function in Health and Disease 2.0)
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23 pages, 940 KiB  
Review
Crosstalk among Calcium ATPases: PMCA, SERCA and SPCA in Mental Diseases
by Tomasz Boczek, Marta Sobolczyk, Joanna Mackiewicz, Malwina Lisek, Bozena Ferenc, Feng Guo and Ludmila Zylinska
Int. J. Mol. Sci. 2021, 22(6), 2785; https://doi.org/10.3390/ijms22062785 - 10 Mar 2021
Cited by 8 | Viewed by 3866
Abstract
Calcium in mammalian neurons is essential for developmental processes, neurotransmitter release, apoptosis, and signal transduction. Incorrectly processed Ca2+ signal is well-known to trigger a cascade of events leading to altered response to variety of stimuli and persistent accumulation of pathological changes at [...] Read more.
Calcium in mammalian neurons is essential for developmental processes, neurotransmitter release, apoptosis, and signal transduction. Incorrectly processed Ca2+ signal is well-known to trigger a cascade of events leading to altered response to variety of stimuli and persistent accumulation of pathological changes at the molecular level. To counterbalance potentially detrimental consequences of Ca2+, neurons are equipped with sophisticated mechanisms that function to keep its concentration in a tightly regulated range. Calcium pumps belonging to the P-type family of ATPases: plasma membrane Ca2+-ATPase (PMCA), sarco/endoplasmic Ca2+-ATPase (SERCA) and secretory pathway Ca2+-ATPase (SPCA) are considered efficient line of defense against abnormal Ca2+ rises. However, their role is not limited only to Ca2+ transport, as they present tissue-specific functionality and unique sensitive to the regulation by the main calcium signal decoding protein—calmodulin (CaM). Based on the available literature, in this review we analyze the contribution of these three types of Ca2+-ATPases to neuropathology, with a special emphasis on mental diseases. Full article
(This article belongs to the Special Issue Calmodulin Function in Health and Disease 2.0)
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26 pages, 1037 KiB  
Review
Structural Aspects and Prediction of Calmodulin-Binding Proteins
by Corey Andrews, Yiting Xu, Michael Kirberger and Jenny J. Yang
Int. J. Mol. Sci. 2021, 22(1), 308; https://doi.org/10.3390/ijms22010308 - 30 Dec 2020
Cited by 23 | Viewed by 3716
Abstract
Calmodulin (CaM) is an important intracellular protein that binds Ca2+ and functions as a critical second messenger involved in numerous biological activities through extensive interactions with proteins and peptides. CaM’s ability to adapt to binding targets with different structures is related to [...] Read more.
Calmodulin (CaM) is an important intracellular protein that binds Ca2+ and functions as a critical second messenger involved in numerous biological activities through extensive interactions with proteins and peptides. CaM’s ability to adapt to binding targets with different structures is related to the flexible central helix separating the N- and C-terminal lobes, which allows for conformational changes between extended and collapsed forms of the protein. CaM-binding targets are most often identified using prediction algorithms that utilize sequence and structural data to predict regions of peptides and proteins that can interact with CaM. In this review, we provide an overview of different CaM-binding proteins, the motifs through which they interact with CaM, and shared properties that make them good binding partners for CaM. Additionally, we discuss the historical and current methods for predicting CaM binding, and the similarities and differences between these methods and their relative success at prediction. As new CaM-binding proteins are identified and classified, we will gain a broader understanding of the biological processes regulated through changes in Ca2+ concentration through interactions with CaM. Full article
(This article belongs to the Special Issue Calmodulin Function in Health and Disease 2.0)
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Graphical abstract

38 pages, 2443 KiB  
Review
Pleiotropic Roles of Calmodulin in the Regulation of KRas and Rac1 GTPases: Functional Diversity in Health and Disease
by Francesc Tebar, Albert Chavero, Neus Agell, Albert Lu, Carles Rentero, Carlos Enrich and Thomas Grewal
Int. J. Mol. Sci. 2020, 21(10), 3680; https://doi.org/10.3390/ijms21103680 - 23 May 2020
Cited by 9 | Viewed by 4105
Abstract
Calmodulin is a ubiquitous signalling protein that controls many biological processes due to its capacity to interact and/or regulate a large number of cellular proteins and pathways, mostly in a Ca2+-dependent manner. This complex interactome of calmodulin can have pleiotropic molecular [...] Read more.
Calmodulin is a ubiquitous signalling protein that controls many biological processes due to its capacity to interact and/or regulate a large number of cellular proteins and pathways, mostly in a Ca2+-dependent manner. This complex interactome of calmodulin can have pleiotropic molecular consequences, which over the years has made it often difficult to clearly define the contribution of calmodulin in the signal output of specific pathways and overall biological response. Most relevant for this review, the ability of calmodulin to influence the spatiotemporal signalling of several small GTPases, in particular KRas and Rac1, can modulate fundamental biological outcomes such as proliferation and migration. First, direct interaction of calmodulin with these GTPases can alter their subcellular localization and activation state, induce post-translational modifications as well as their ability to interact with effectors. Second, through interaction with a set of calmodulin binding proteins (CaMBPs), calmodulin can control the capacity of several guanine nucleotide exchange factors (GEFs) to promote the switch of inactive KRas and Rac1 to an active conformation. Moreover, Rac1 is also an effector of KRas and both proteins are interconnected as highlighted by the requirement for Rac1 activation in KRas-driven tumourigenesis. In this review, we attempt to summarize the multiple layers how calmodulin can regulate KRas and Rac1 GTPases in a variety of cellular events, with biological consequences and potential for therapeutic opportunities in disease settings, such as cancer. Full article
(This article belongs to the Special Issue Calmodulin Function in Health and Disease 2.0)
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