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Analysis of cholesterol-recognition motifs of the plasma membrane Ca2+-ATPase.

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Title: Analysis of cholesterol-recognition motifs of the plasma membrane Ca2+-ATPase.
Authors: Delgado-Coello, Blanca1 (AUTHOR) bdelgado@ifc.unam.mx, Luna-Reyes, Ismael1 (AUTHOR), Méndez-Acevedo, Kevin M.1,2 (AUTHOR), Bravo-Martínez, Jorge3 (AUTHOR), Montalvan-Sorrosa, Danai4 (AUTHOR), Mas-Oliva, Jaime1 (AUTHOR) jmas@ifc.unam.mx
Source: Journal of Bioenergetics & Biomembranes. Jun2024, Vol. 56 Issue 3, p205-219. 15p.
Subjects: Cell membranes, Transmembrane domains, Membrane lipids, Molecular dynamics, Cholesterol, Intracellular calcium, Adenosine triphosphatase
Abstract: The plasma membrane Ca2+-ATPase (PMCA) is crucial for the fine tuning of intracellular calcium levels in eukaryotic cells. In this study, we show the presence of CARC sequences in all human and rat PMCA isoforms and we performed further analysis by molecular dynamics simulations. This analysis focuses on PMCA1, containing three CARC motifs, and PMCA4, with four CARC domains. In PMCA1, two CARC motifs reside within transmembrane domains, while the third is situated at the intracellular interface. The simulations depict more stable RMSD values and lower RMSF fluctuations in the presence of cholesterol, emphasizing its potential stabilizing effect. In PMCA4, a distinct dynamic was found. Notably, the total energy differences between simulations with cholesterol and phospholipids are pronounced in PMCA4 compared to PMCA1. RMSD values for PMCA4 indicate a more energetically favorable conformation in the presence of cholesterol, suggesting a robust interaction between CARCs and this lipid in the membranes. Furthermore, RMSF analysis for CARCs in both PMCA isoforms exhibit lower values in the presence of cholesterol compared to POPC alone. The analysis of H-bond occupancy and total energy values strongly suggests the potential interaction of CARCs with cholesterol. Given the crucial role of PMCAs in physiological calcium regulation and their involvement in diverse pathological processes, this study underscores the significance of CARC motifs and their interaction with cholesterol in elucidating PMCA function. These insights into the energetic preferences associated with CARC-cholesterol interactions offer valuable implications for understanding PMCA function in maintaining calcium homeostasis and addressing potential associated pathologies. [ABSTRACT FROM AUTHOR]
Copyright of Journal of Bioenergetics & Biomembranes is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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  Data: Analysis of cholesterol-recognition motifs of the plasma membrane Ca<superscript>2+</superscript>-ATPase.
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  Data: <searchLink fieldCode="AR" term="%22Delgado-Coello%2C+Blanca%22">Delgado-Coello, Blanca</searchLink><relatesTo>1</relatesTo> (AUTHOR)<i> bdelgado@ifc.unam.mx</i><br /><searchLink fieldCode="AR" term="%22Luna-Reyes%2C+Ismael%22">Luna-Reyes, Ismael</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Méndez-Acevedo%2C+Kevin+M%2E%22">Méndez-Acevedo, Kevin M.</searchLink><relatesTo>1,2</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Bravo-Martínez%2C+Jorge%22">Bravo-Martínez, Jorge</searchLink><relatesTo>3</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Montalvan-Sorrosa%2C+Danai%22">Montalvan-Sorrosa, Danai</searchLink><relatesTo>4</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Mas-Oliva%2C+Jaime%22">Mas-Oliva, Jaime</searchLink><relatesTo>1</relatesTo> (AUTHOR)<i> jmas@ifc.unam.mx</i>
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  Data: <searchLink fieldCode="JN" term="%22Journal+of+Bioenergetics+%26+Biomembranes%22">Journal of Bioenergetics & Biomembranes</searchLink>. Jun2024, Vol. 56 Issue 3, p205-219. 15p.
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  Data: <searchLink fieldCode="DE" term="%22Cell+membranes%22">Cell membranes</searchLink><br /><searchLink fieldCode="DE" term="%22Transmembrane+domains%22">Transmembrane domains</searchLink><br /><searchLink fieldCode="DE" term="%22Membrane+lipids%22">Membrane lipids</searchLink><br /><searchLink fieldCode="DE" term="%22Molecular+dynamics%22">Molecular dynamics</searchLink><br /><searchLink fieldCode="DE" term="%22Cholesterol%22">Cholesterol</searchLink><br /><searchLink fieldCode="DE" term="%22Intracellular+calcium%22">Intracellular calcium</searchLink><br /><searchLink fieldCode="DE" term="%22Adenosine+triphosphatase%22">Adenosine triphosphatase</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: The plasma membrane Ca2+-ATPase (PMCA) is crucial for the fine tuning of intracellular calcium levels in eukaryotic cells. In this study, we show the presence of CARC sequences in all human and rat PMCA isoforms and we performed further analysis by molecular dynamics simulations. This analysis focuses on PMCA1, containing three CARC motifs, and PMCA4, with four CARC domains. In PMCA1, two CARC motifs reside within transmembrane domains, while the third is situated at the intracellular interface. The simulations depict more stable RMSD values and lower RMSF fluctuations in the presence of cholesterol, emphasizing its potential stabilizing effect. In PMCA4, a distinct dynamic was found. Notably, the total energy differences between simulations with cholesterol and phospholipids are pronounced in PMCA4 compared to PMCA1. RMSD values for PMCA4 indicate a more energetically favorable conformation in the presence of cholesterol, suggesting a robust interaction between CARCs and this lipid in the membranes. Furthermore, RMSF analysis for CARCs in both PMCA isoforms exhibit lower values in the presence of cholesterol compared to POPC alone. The analysis of H-bond occupancy and total energy values strongly suggests the potential interaction of CARCs with cholesterol. Given the crucial role of PMCAs in physiological calcium regulation and their involvement in diverse pathological processes, this study underscores the significance of CARC motifs and their interaction with cholesterol in elucidating PMCA function. These insights into the energetic preferences associated with CARC-cholesterol interactions offer valuable implications for understanding PMCA function in maintaining calcium homeostasis and addressing potential associated pathologies. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Journal of Bioenergetics & Biomembranes is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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RecordInfo BibRecord:
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      – Type: doi
        Value: 10.1007/s10863-024-10010-5
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      – Code: eng
        Text: English
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        PageCount: 15
        StartPage: 205
    Subjects:
      – SubjectFull: Cell membranes
        Type: general
      – SubjectFull: Transmembrane domains
        Type: general
      – SubjectFull: Membrane lipids
        Type: general
      – SubjectFull: Molecular dynamics
        Type: general
      – SubjectFull: Cholesterol
        Type: general
      – SubjectFull: Intracellular calcium
        Type: general
      – SubjectFull: Adenosine triphosphatase
        Type: general
    Titles:
      – TitleFull: Analysis of cholesterol-recognition motifs of the plasma membrane Ca2+-ATPase.
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            NameFull: Delgado-Coello, Blanca
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            NameFull: Luna-Reyes, Ismael
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            NameFull: Méndez-Acevedo, Kevin M.
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            – D: 01
              M: 06
              Text: Jun2024
              Type: published
              Y: 2024
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