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Ion Pathways in the Sarcoplasmic Reticulum Ca2+-ATPase.

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Title: Ion Pathways in the Sarcoplasmic Reticulum Ca2+-ATPase.
Authors: Bublitz, Maike1,2 mbu@mb.au.dk, Musgaard, Maria1,3, Poulsen, Hanne1,2, Thøgersen, Lea1,4, Olesen, Claus1,5, Schiøtt, Birgit1,6,7, Preben Morth, J.1,2, Møller, Jesper Vuust1,5, Nissen, Poul1,2
Source: Journal of Biological Chemistry. 4/12/2013, Vol. 288 Issue 15, p10759-10765. 7p.
Subjects: Sarcoplasmic reticulum, Endoplasmic reticulum, Adenosine triphosphatase, Muscle contraction, Bilayer lipid membranes, Ion exchange (Chemistry)
Abstract: The sarco/endoplasmic reticulum Ca2+-ATPase (SERCA) is a transmembrane ion transporter belonging to the PII-type ATPase family. It performs the vital task of re-sequestering cytoplasmic Ca2+ to the sarco/endoplasmic reticulum store, thereby also terminating Ca2+-induced signaling such as in muscle contraction. This minireview focuses on the transport pathways of Ca2+ and H+ ions across the lipid bilayer through SERCA. The ion-binding sites of SERCA are accessible from either the cytoplasm or the sarco/endoplasmic reticulum lumen, and the Ca2+ entry and exit channels are both formed mainly by rearrangements of four N-terminal transmembrane α-helices. Recent improvements in the resolution of the crystal structures of rabbit SERCA1a have revealed a hydrated pathway in the C-terminal transmembrane region leading from the ionbinding sites to the cytosol. A comparison of different SERCA conformations reveals that this C-terminal pathway is exclusive to Ca2+-free E2 states, suggesting that it may play a functional role in proton release from the ion-binding sites. This is in agreement with molecular dynamics simulations and mutational studies and is in striking analogy to a similar pathway recently described for the related sodium pump. We therefore suggest a model for the ion exchange mechanism in PII-ATPases including not one, but two cytoplasmic pathways working in concert. [ABSTRACT FROM AUTHOR]
Copyright of Journal of Biological Chemistry is the property of Elsevier B.V. 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.)
Database: Engineering Source
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Header DbId: egs
DbLabel: Engineering Source
An: 87415999
AccessLevel: 6
PubType: Academic Journal
PubTypeId: academicJournal
PreciseRelevancyScore: 0
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  Label: Title
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  Data: Ion Pathways in the Sarcoplasmic Reticulum Ca<superscript>2+</superscript>-ATPase.
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  Data: <searchLink fieldCode="AR" term="%22Bublitz%2C+Maike%22">Bublitz, Maike</searchLink><relatesTo>1,2</relatesTo><i> mbu@mb.au.dk</i><br /><searchLink fieldCode="AR" term="%22Musgaard%2C+Maria%22">Musgaard, Maria</searchLink><relatesTo>1,3</relatesTo><br /><searchLink fieldCode="AR" term="%22Poulsen%2C+Hanne%22">Poulsen, Hanne</searchLink><relatesTo>1,2</relatesTo><br /><searchLink fieldCode="AR" term="%22Thøgersen%2C+Lea%22">Thøgersen, Lea</searchLink><relatesTo>1,4</relatesTo><br /><searchLink fieldCode="AR" term="%22Olesen%2C+Claus%22">Olesen, Claus</searchLink><relatesTo>1,5</relatesTo><br /><searchLink fieldCode="AR" term="%22Schiøtt%2C+Birgit%22">Schiøtt, Birgit</searchLink><relatesTo>1,6,7</relatesTo><br /><searchLink fieldCode="AR" term="%22Preben+Morth%2C+J%2E%22">Preben Morth, J.</searchLink><relatesTo>1,2</relatesTo><br /><searchLink fieldCode="AR" term="%22Møller%2C+Jesper+Vuust%22">Møller, Jesper Vuust</searchLink><relatesTo>1,5</relatesTo><br /><searchLink fieldCode="AR" term="%22Nissen%2C+Poul%22">Nissen, Poul</searchLink><relatesTo>1,2</relatesTo>
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  Data: <searchLink fieldCode="JN" term="%22Journal+of+Biological+Chemistry%22">Journal of Biological Chemistry</searchLink>. 4/12/2013, Vol. 288 Issue 15, p10759-10765. 7p.
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  Data: <searchLink fieldCode="DE" term="%22Sarcoplasmic+reticulum%22">Sarcoplasmic reticulum</searchLink><br /><searchLink fieldCode="DE" term="%22Endoplasmic+reticulum%22">Endoplasmic reticulum</searchLink><br /><searchLink fieldCode="DE" term="%22Adenosine+triphosphatase%22">Adenosine triphosphatase</searchLink><br /><searchLink fieldCode="DE" term="%22Muscle+contraction%22">Muscle contraction</searchLink><br /><searchLink fieldCode="DE" term="%22Bilayer+lipid+membranes%22">Bilayer lipid membranes</searchLink><br /><searchLink fieldCode="DE" term="%22Ion+exchange+%28Chemistry%29%22">Ion exchange (Chemistry)</searchLink>
– Name: Abstract
  Label: Abstract
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  Data: The sarco/endoplasmic reticulum Ca2+-ATPase (SERCA) is a transmembrane ion transporter belonging to the PII-type ATPase family. It performs the vital task of re-sequestering cytoplasmic Ca2+ to the sarco/endoplasmic reticulum store, thereby also terminating Ca2+-induced signaling such as in muscle contraction. This minireview focuses on the transport pathways of Ca2+ and H+ ions across the lipid bilayer through SERCA. The ion-binding sites of SERCA are accessible from either the cytoplasm or the sarco/endoplasmic reticulum lumen, and the Ca2+ entry and exit channels are both formed mainly by rearrangements of four N-terminal transmembrane α-helices. Recent improvements in the resolution of the crystal structures of rabbit SERCA1a have revealed a hydrated pathway in the C-terminal transmembrane region leading from the ionbinding sites to the cytosol. A comparison of different SERCA conformations reveals that this C-terminal pathway is exclusive to Ca2+-free E2 states, suggesting that it may play a functional role in proton release from the ion-binding sites. This is in agreement with molecular dynamics simulations and mutational studies and is in striking analogy to a similar pathway recently described for the related sodium pump. We therefore suggest a model for the ion exchange mechanism in PII-ATPases including not one, but two cytoplasmic pathways working in concert. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Journal of Biological Chemistry is the property of Elsevier B.V. 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: 10.1074/jbc.R112.436550
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      – Code: eng
        Text: English
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      Pagination:
        PageCount: 7
        StartPage: 10759
    Subjects:
      – SubjectFull: Sarcoplasmic reticulum
        Type: general
      – SubjectFull: Endoplasmic reticulum
        Type: general
      – SubjectFull: Adenosine triphosphatase
        Type: general
      – SubjectFull: Muscle contraction
        Type: general
      – SubjectFull: Bilayer lipid membranes
        Type: general
      – SubjectFull: Ion exchange (Chemistry)
        Type: general
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      – TitleFull: Ion Pathways in the Sarcoplasmic Reticulum Ca2+-ATPase.
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              M: 04
              Text: 4/12/2013
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              Y: 2013
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