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Life
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Protein Phosphorylation: Mechanism and Regulation
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Protein Phosphorylation: Mechanism and Regulation

A special issue of Life (ISSN 2075-1729). This special issue belongs to the section "Proteins and Proteomics".

Deadline for manuscript submissions: closed (31 October 2022) | Viewed by 13897

Special Issue Editor

Dr. Xin Li

E-Mail Website
Guest Editor
Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Beijing 100193, China
Interests: meat science; protein phosphorylation; energy metabolism; protein post-translational modification crosstalk
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Reversible protein phosphorylation is one of the most important post-translational modifications, which plays essential roles in biological activities, such as gene expression, cell proliferation, signal transduction, etc. About one-third of proteins are presumed to be phosphorylated in eucaryote. Phosphorylation modifies enzymatic activity, protein structure, interaction, and localization. More elaborate and complicated regulation networks have been revealed to control the birth and death of cells since the discovery of protein phosphorylation. ATP-dependent protein phosphorylation is closely regulated by energy metabolism and, in turn, it also regulates energy metabolism through changing enzyme/protein functions. Mitochondria is famous as an energy house and it may carry out apoptosis when cells undergo stress. Protein phosphorylation performs critical regulatory roles in this complex process through altering protein behavior. In addition, the inhibitors or activators of protein kinases or phosphatases are always used to regulate signal transduction, such as the well-understood mTOR and MAPK signaling pathways. As the development of mass spectrometric technology, proteins are identified with more multiply modifications besides phosphorylation. The positive or negative crosstalk between protein phosphorylation and other post-translational modifications adds more complexity to investigate cellular activities.

This Special Issue aims to communicate latest research outcomes from various fields on the roles of protein phosphorylation in the regulation of protein functions. High-quality papers within the journal’s scope, including original research reviews and articles, are welcome.

Dr. Xin Li
Guest Editor

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Keywords

  • protein phosphorylation
  • energy metabolism
  • protein post-translational modifications crosstalk
  • apoptosis
  • protein kinase

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Published Papers (4 papers)

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Research

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12 pages, 2748 KiB  
Article
Phosphorylation of Calpastatin Negatively Regulates the Activity of Calpain
by Yuqiang Bai, Chengli Hou, Caiyan Huang, Fei Fang, Yu Dong, Xin Li and Dequan Zhang
Life 2023, 13(3), 854; https://doi.org/10.3390/life13030854 - 22 Mar 2023
Cited by 4 | Viewed by 1974
Abstract
Tenderness is an important characteristic of meat quality. Calpastatin and calpain play important roles in meat tenderization. However, it is not clear how phosphorylation affects the regulation of calpastatin on μ-calpain and, consequently, meat tenderness. Calpastatin with high and low phosphorylation levels were [...] Read more.
Tenderness is an important characteristic of meat quality. Calpastatin and calpain play important roles in meat tenderization. However, it is not clear how phosphorylation affects the regulation of calpastatin on μ-calpain and, consequently, meat tenderness. Calpastatin with high and low phosphorylation levels were obtained in vitro corresponding to the treatments by protein kinase A (PKA) and alkaline phosphatase. Then, calpain was incubated with calpastatin with different phosphorylation levels, and the effect of calpastatin on calpain activity under different phosphorylation levels was analyzed. The results showed that PKA promoted the phosphorylation of calpastatin, and a high phosphorylation level was maintained during incubation. The degradation rate of μ-calpain in AP group was higher than that in the other groups, meaning there was lower inhibition of calpastatin on calpain activity. The degradation of calpastatin was lower and its structure was more stable after phosphorylation. One more serine 133 site of calpastatin was identified in PKA group compared with the other groups. Phosphorylation at serine 133 of calpastatin enhanced its inhibition on calpain activity by maintaining its structural stability, thus inhibiting the tenderization of meat. Full article
(This article belongs to the Special Issue Protein Phosphorylation: Mechanism and Regulation)
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13 pages, 10712 KiB  
Article
Phosphorylation and Dephosphorylation of Beta-Amyloid Peptide in Model Cell Cultures: The Role of Cellular Protein Kinases and Phosphatases
by Evgeny P. Barykin, Dmitry V. Yanvarev, Maria A. Strelkova, Vladimir T. Valuev-Elliston, Kseniya B. Varshavskaya, Vladimir A. Mitkevich and Alexander A. Makarov
Life 2023, 13(1), 147; https://doi.org/10.3390/life13010147 - 4 Jan 2023
Cited by 2 | Viewed by 1879
Abstract
Phosphorylation of beta-amyloid peptide (Aβ) at the Ser8 residue affects its neurotoxicity, metal-dependent oligomerisation, amyloidogenicity, and other pathogenic properties. Phosphorylated Aβ (pS8-Aβ) was detected in vivo in AD model mice and in the brains of patients with AD. However, the pS8-Aβ production and [...] Read more.
Phosphorylation of beta-amyloid peptide (Aβ) at the Ser8 residue affects its neurotoxicity, metal-dependent oligomerisation, amyloidogenicity, and other pathogenic properties. Phosphorylated Aβ (pS8-Aβ) was detected in vivo in AD model mice and in the brains of patients with AD. However, the pS8-Aβ production and the regulation of its levels have not been previously studied in detail. In this paper, immunochemical methods together with radioactive labelling were used to study the Aβ phosphorylation by intracellular and surface protein kinases of HEK293 cells and brain endothelial cells (bEnd.3). It was found that HEK293 robustly phosphorylated Aβ, likely with contribution from casein kinase 2 (CK2), whereas in bEnd.3, the activity of Aβ phosphorylation was relatively low. Further, the study showed that both HEK293 and bEnd.3 could dephosphorylate pS8-Aβ, mainly due to the activity of protein phosphatases PP1 and PP2A. The Aβ dephosphorylation efficiency in bEnd.3 was three times higher than in HEK293, which correlated with the reduced abundance of pS8-Aβ in vascular amyloid deposits of patients with AD compared to senile plaques. These data suggest an important role of CK2, PP1, and PP2A as regulators of Aβ phosphorylation, and point to the involvement of the blood–brain barrier in the control of Aβ modification levels. Full article
(This article belongs to the Special Issue Protein Phosphorylation: Mechanism and Regulation)
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19 pages, 3188 KiB  
Article
ABA-Dependent Regulation of Calcium-Dependent Protein Kinase Gene GmCDPK5 in Cultivated and Wild Soybeans
by Galina N. Veremeichik, Evgenia V. Brodovskaya, Valeria P. Grigorchuk, Ekaterina S. Butovets, Ludmila M. Lukyanchuk and Victor P. Bulgakov
Life 2022, 12(10), 1576; https://doi.org/10.3390/life12101576 - 11 Oct 2022
Cited by 3 | Viewed by 2002
Abstract
Calcium-dependent protein kinases (CDPKs) regulate plant development and stress responses. However, the interaction of these protein kinases with the abscisic acid (ABA) stress hormone signalling system has not been studied in detail. In Arabidopsis, AtCPK1 plays an important role in the acclimation [...] Read more.
Calcium-dependent protein kinases (CDPKs) regulate plant development and stress responses. However, the interaction of these protein kinases with the abscisic acid (ABA) stress hormone signalling system has not been studied in detail. In Arabidopsis, AtCPK1 plays an important role in the acclimation of plants to environmental stresses. Phylogenetic and molecular analyses showed that, among 50 isoforms of Glycine max (L.) Merrill CDPKs, the GmCDPK27/GmCDPK48, GmCDPK5/GmCDPK24, and GmCDPK10/GmCDPK46 paralogous pairs were the isoforms most related to AtCDPK1. We investigated the expression of the corresponding six GmCDPKs genes during treatment with cold, heat, and salt stress. Wild soybean was the most resistant to stresses, and among the three cultivars studied (Sfera, Hodgson, and Hefeng25), Sfera was close to the wild type in terms of resistance. GmCDPK5 and GmCDPK10 were the most responsive to stress treatments, especially in wild soybean, compared with cultivars. Among the studied GmCDPK isoforms, only GmCDPK5 expression increased after treatment with abscisic acid (ABA) in a dose- and time-dependent manner. Targeted LC-MS/MS analysis of endogenous ABA levels showed that wild soybean and Sfera had nearly twice the ABA content of Hodgson and Hefeng25. An analysis of the expression of marker genes involved in ABA biosynthesis showed that GmNCED1-gene-encoding 9-cis-epoxycarotenoid dioxygenase 1 is induced to the greatest extent in wild soybean and Sfera under salt, cold, and heat exposure. Our data established a correlation between the induction of GmCDPK5 and ABA biosynthesis genes. GmCDPK5 is an interesting target for genetic and bioengineering purposes and can be used for genetic editing, overexpression, or as a marker gene in soybean varieties growing under unfavourable conditions. Full article
(This article belongs to the Special Issue Protein Phosphorylation: Mechanism and Regulation)
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Review

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14 pages, 1740 KiB  
Review
Functional Insights into Protein Kinase A (PKA) Signaling from C. elegans
by Fereshteh Sadeghian, Perla G. Castaneda, Mustafi R. Amin and Erin J. Cram
Life 2022, 12(11), 1878; https://doi.org/10.3390/life12111878 - 14 Nov 2022
Cited by 3 | Viewed by 7032
Abstract
Protein kinase A (PKA), which regulates a diverse set of biological functions downstream of cyclic AMP (cAMP), is a tetramer consisting of two catalytic subunits (PKA-C) and two regulatory subunits (PKA-R). When cAMP binds the PKA-R subunits, the PKA-C subunits are released and [...] Read more.
Protein kinase A (PKA), which regulates a diverse set of biological functions downstream of cyclic AMP (cAMP), is a tetramer consisting of two catalytic subunits (PKA-C) and two regulatory subunits (PKA-R). When cAMP binds the PKA-R subunits, the PKA-C subunits are released and interact with downstream effectors. In Caenorhabditis elegans (C. elegans), PKA-C and PKA-R are encoded by kin-1 and kin-2, respectively. This review focuses on the contributions of work in C. elegans to our understanding of the many roles of PKA, including contractility and oocyte maturation in the reproductive system, lipid metabolism, physiology, mitochondrial function and lifespan, and a wide variety of behaviors. C. elegans provides a powerful genetic platform for understanding how this kinase can regulate an astounding variety of physiological responses. Full article
(This article belongs to the Special Issue Protein Phosphorylation: Mechanism and Regulation)
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