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Calcium-Binding Proteins and Cell Signaling, 4th Edition
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Calcium-Binding Proteins and Cell Signaling, 4th Edition

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

Deadline for manuscript submissions: closed (20 April 2025) | Viewed by 1153

Special Issue Editor

Dr. Hideki Shibata

E-Mail Website
Guest Editor
Department of Applied Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, Japan
Interests: calcium-binding protein; membrane traffic
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Calcium ions play pivotal roles in a variety of cellular events, including signal transduction, gene expression, cell death, fertilization, muscle contraction, membrane fusion, blood clotting, enzymatic activations of kinases, phosphatases, proteases, etc., by involving different kinds of calcium-binding proteins. The concentrations of Ca2+ in the blood and inside cells are strictly regulated by Ca2+-sensing proteins, channels, and transporters and Ca2+-buffering proteins. In addition to the sarcoplasmic/endoplasmic reticulum, known as the major Ca2+-storage organelle in the cell, mitochondria, Golgi apparatus, endosomes, and lysosomes are also known to play roles in Ca2+ signaling. The nuclear roles of Ca2+ in transcriptional and post-transcriptional regulation are also drawing attention. Ca2+ works not only as a second messenger but also as a first messenger for Ca2+-sensing receptors located on the plasma membrane. Abnormalities in Ca2+ homeostasis or in the functions of Ca2+-regulated factors cause, directly or indirectly, various diseases, such as neuropathies, heart failure, immune disorders, and osteogenesis imperfecta. Ca2+-dependent phenomena are not restricted to animals; plants, lower eukaryotes, and some bacteria also use Ca2+ as a signaling molecule.

As volumes 1, 2, and 3 of Special Issues “Calcium-Binding Proteins and Cell Signaling” are successful, we reopen this issue again in the International Journal of Molecular Sciences (https://www.mdpi.com/journal/ijms, ISSN 1422-0067, IF 5.924, JCR Category Q1). This forth Special Issue, “Calcium-Binding Proteins and Cell Signaling, 4th Edition”, welcomes contributions covering all areas of basic and application-oriented research associated with calcium regarding the aspects of biochemistry, cell biology, molecular biology, and biophysics.

Dr. Hideki Shibata
Guest Editor

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Research

16 pages, 3494 KB  
Article
A Unique Insertion Loop Facilitates Tight NAD+ Binding in Nicotinoprotein: Insights from In Vitro Loop Engineering and In Silico Studies
by Houcheng Xue, Takumi Yanase, Junko Okuda-Shimazaki, Haruka Kawai, Daimei Miura, Ryutaro Asano, Kazunori Ikebukuro, Koji Sode and Wakako Tsugawa
Int. J. Mol. Sci. 2026, 27(5), 2367; https://doi.org/10.3390/ijms27052367 - 3 Mar 2026
Viewed by 458
Abstract
Nicotinoproteins are a group of NAD+-dependent dehydrogenases that bind NAD+ tightly and catalyze reactions without using free NAD+. In this study, we investigated the role of the unique insertion loop in nicotinoproteins. Carveol dehydrogenase (CADh), a short-chain dehydrogenase/reductase [...] Read more.
Nicotinoproteins are a group of NAD+-dependent dehydrogenases that bind NAD+ tightly and catalyze reactions without using free NAD+. In this study, we investigated the role of the unique insertion loop in nicotinoproteins. Carveol dehydrogenase (CADh), a short-chain dehydrogenase/reductase (SDR) nicotinoprotein, and β-hydroxybutyrate dehydrogenase from Alcaligenes faecalis (AfBHBDh), a non-nicotinoprotein counterpart, were used as model enzymes. An insertion loop-deleted mutant, CADh Δ39–49, was constructed. An insertion loop from Mycobacterium paratuberculosis CADh (MpCADh) was introduced into AfBHBDh to generate the two mutants. The results showed that CADh Δ39–49 lost NAD+ tight binding capacity and could not utilize free NAD+. In contrast, the AfBHBDh mutants showed no dye-mediated dehydrogenase activity. Moreover, the KM and KD values for NAD+ were higher than those of the wild-type enzyme. Docking simulations revealed a stronger binding affinity between NAD+ and the mutants than with the wild-type AfBHBDh. Taken together, these results suggest that the insertion loop interferes with NAD+ entry into the active site of the enzyme while creating a more energetically favorable binding environment. This loop is necessary but alone is insufficient to achieve NAD+ tight binding. This study deepens understanding of NAD+ binding in SDR nicotinoproteins and provides insights for SDR enzyme engineering. Full article
(This article belongs to the Special Issue Calcium-Binding Proteins and Cell Signaling, 4th Edition)
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