P-type ATPases: Many more enigmas left to solve

Palmgren, Michael

doi:10.1016/j.jbc.2023.105352

Cited by 19 publications

(6 citation statements)

References 205 publications

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“…The phylogenetic analysis carried out here has also made it possible to verify that some proteins initially proposed in the literature as ENA ATPases do not seem to belong to this group of P-ATPases since, although they show a certain phylogenetic proximity, they form a separate clade. In this regard, a recent paper describes the identification of a new family of P-ATPases present in some bacteria, which are not assigned to any of the five P1-P5 families and which have constituted a new clade called P6 [ 30 ]. Similarly, our results could suggest that the P2-type ATPase subfamily could be divided into more groups than are currently considered.…”

Section: Discussionmentioning

confidence: 99%

Phylogenetic and Structure-Function Analyses of ENA ATPases: A Case Study of the ENA1 Protein from the Fungus Neurospora crassa

Aguilella,

Garciadeblás,

Fernández Pacios

et al. 2023

IJMS

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ENA transporters are a group of P-type ATPases that are characterized by actively moving Na+ or K+ out of the cell against their concentration gradient. The existence of these transporters was initially attributed to some fungi, although more recently they have also been identified in mosses, liverworts, and some protozoa. Given the current increase in the number of organisms whose genomes are completely sequenced, we set out to expand our knowledge about the existence of ENA in organisms belonging to other phylogenetic groups. For that, a hidden Markov model profile was constructed to identify homologous sequences to ENA proteins in protein databases. This analysis allowed us to identify the existence of ENA-type ATPases in the most primitive groups of fungi, as well as in other eukaryotic organisms not described so far. In addition, this study has allowed the identification of a possible new group of P-ATPases, initially proposed as ENA but which maintain phylogenetic distances with these proteins. Finally, this work has also addressed this study of the structure of ENA proteins, which remained unknown due to the lack of crystallographic data. For this purpose, a 3D structure prediction of the NcENA1 protein of the fungus Neurospora crassa was performed using AlphaFold2 software v2.3.1. From this structure, the electrostatic potential of the protein was analyzed. With all these data, the protein regions and the amino acids involved in the transport of Na+ or K+ ions across the membrane were proposed for the first time. Targeted mutagenesis of some of these residues has confirmed their relevant participation in the transport function of ENA proteins.

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Section: Discussionmentioning

confidence: 99%

Phylogenetic and Structure-Function Analyses of ENA ATPases: A Case Study of the ENA1 Protein from the Fungus Neurospora crassa

Aguilella,

Garciadeblás,

Fernández Pacios

et al. 2023

IJMS

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“…NKA is classified as a member of the superfamily of P-type ATPases, which transport various compounds vectorially, ranging from H + to phospholipids, at the expense of ATP [ 60 ]. Due to its structural and functional characteristics, NKA is categorized as a type IIC-ATPase, sharing close relatives, such as H+/K + -ATPase and the sarcoplasmic/endoplasmic reticulum Ca2+-ATPase (SERCA) [ 61 , 62 , 63 , 64 ].…”

Section: Nka’s Role As An Electrogenic Pumpmentioning

confidence: 99%

Na+/K+-ATPase: More than an Electrogenic Pump

Contreras,

Torres-Carrillo,

Flores-Maldonado

et al. 2024

IJMS

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The sodium pump, or Na+/K+-ATPase (NKA), is an essential enzyme found in the plasma membrane of all animal cells. Its primary role is to transport sodium (Na+) and potassium (K+) ions across the cell membrane, using energy from ATP hydrolysis. This transport creates and maintains an electrochemical gradient, which is crucial for various cellular processes, including cell volume regulation, electrical excitability, and secondary active transport. Although the role of NKA as a pump was discovered and demonstrated several decades ago, it remains the subject of intense research. Current studies aim to delve deeper into several aspects of this molecular entity, such as describing its structure and mode of operation in atomic detail, understanding its molecular and functional diversity, and examining the consequences of its malfunction due to structural alterations. Additionally, researchers are investigating the effects of various substances that amplify or decrease its pumping activity. Beyond its role as a pump, growing evidence indicates that in various cell types, NKA also functions as a receptor for cardiac glycosides like ouabain. This receptor activity triggers the activation of various signaling pathways, producing significant morphological and physiological effects. In this report, we present the results of a comprehensive review of the most outstanding studies of the past five years. We highlight the progress made regarding this new concept of NKA and the various cardiac glycosides that influence it. Furthermore, we emphasize NKA’s role in epithelial physiology, particularly its function as a receptor for cardiac glycosides that trigger intracellular signals regulating cell–cell contacts, proliferation, differentiation, and adhesion. We also analyze the role of NKA β-subunits as cell adhesion molecules in glia and epithelial cells.

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“…Light-induced stomatal opening is driven by the activation of the plasma membrane (PM) H + -ATPase in guard cells, which generates an electrochemical gradient across the PM to promote ion influx and a consequent turgor increase through osmotic water uptake by the cell ( Shimazaki et al., 2007 ; Inoue and Kinoshita, 2017 ; Fuglsang and Palmgren, 2021 ; Palmgren, 2023 ). The activation of PM H + -ATPase is mediated by the phosphorylation of its C-terminal penultimate residue, threonine (Thr), in guard cells ( Kinoshita and Shimazaki, 1999 , 2002 ).…”

Section: Introductionmentioning

confidence: 99%

A novel semi-dominant mutation in brassinosteroid signaling kinase1 increases stomatal density

Ando,

Taki,

Suzuki

et al. 2024

Front. Plant Sci.

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Stomata play a pivotal role in balancing CO2 uptake for photosynthesis and water loss via transpiration. Thus, appropriate regulation of stomatal movement and its formation are crucial for plant growth and survival. Red and blue light induce phosphorylation of the C-terminal residue of the plasma membrane (PM) H+-ATPase, threonine, in guard cells, generating the driving force for stomatal opening. While significant progress has been made in understanding the regulatory mechanism of PM H+-ATPase in guard cells, the regulatory components for the phosphorylation of PM H+-ATPase have not been fully elucidated. Recently, we established a new immunohistochemical technique for detecting guard-cell PM H+-ATPase phosphorylation using leaves, which was expected to facilitate investigations with a single leaf. In this study, we applied the technique to genetic screening experiment to explore novel regulators for the phosphorylation of PM H+-ATPase in guard cells, as well as stomatal development. We successfully performed phenotyping using a single leaf. During the experiment, we identified a mutant exhibiting high stomatal density, jozetsu (jzt), named after a Japanese word meaning ‘talkative’. We found that a novel semi-dominant mutation in BRASSINOSTEROID SIGNALING KINASE1 (BSK1) is responsible for the phenotype in jzt mutant. The present results demonstrate that the new immunohistochemical technique has a wide range of applications, and the novel mutation would provide genetic tool to expand our understanding of plant development mediated by brassinosteroid signaling.

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P-type ATPases: Many more enigmas left to solve

Cited by 19 publications

References 205 publications

Phylogenetic and Structure-Function Analyses of ENA ATPases: A Case Study of the ENA1 Protein from the Fungus Neurospora crassa

Phylogenetic and Structure-Function Analyses of ENA ATPases: A Case Study of the ENA1 Protein from the Fungus Neurospora crassa

Na+/K+-ATPase: More than an Electrogenic Pump

A novel semi-dominant mutation in brassinosteroid signaling kinase1 increases stomatal density

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