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  Structure of Human Na+/H+ Exchanger NHE1 Regulatory Region in Complex with Calmodulin and Ca2+

Köster, S., Pavkov-Keller, T., Kühlbrandt, W., & Yildiz, Ö. (2011). Structure of Human Na+/H+ Exchanger NHE1 Regulatory Region in Complex with Calmodulin and Ca2+. The Journal of Biological Chemistry, 286(47), 40954-40961. doi:10.1074/jbc.M111.286906.

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 Creators:
Köster, Stefan1, Author           
Pavkov-Keller, Tea1, 2, Author           
Kühlbrandt, Werner1, Author           
Yildiz, Özkan1, Author           
Affiliations:
1Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              
2Department of Structural Biology, Institute of Molecular Biosciences, University of Graz, Humboldtstrasse 50/3, 8010 Graz, Austria, ou_persistent22              

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Free keywords: Calcium-binding Proteins; Calmodulin; Cellular Regulation; Crystal Structure; Membrane Transport; pH Regulation; Sodium Proton Exchange; Structural Biology
 Abstract: The ubiquitous mammalian Na+/H+ exchanger NHE1 has critical functions in regulating intracellular pH, salt concentration, and cellular volume. The regulatory C-terminal domain of NHE1 is linked to the ion-translocating N-terminal membrane domain and acts as a scaffold for signaling complexes. A major interaction partner is calmodulin (CaM), which binds to two neighboring regions of NHE1 in a strongly Ca2+-dependent manner. Upon CaM binding, NHE1 is activated by a shift in sensitivity toward alkaline intracellular pH. Here we report the 2.23 Å crystal structure of the NHE1 CaM binding region (NHE1CaMBR) in complex with CaM and Ca2+. The C- and N-lobes of CaM bind the first and second helix of NHE1CaMBR, respectively. Both the NHE1 helices and the Ca2+-bound CaM are elongated, as confirmed by small angle x-ray scattering analysis. Our x-ray structure sheds new light on the molecular mechanisms of the phosphorylation-dependent regulation of NHE1 and enables us to propose a model of how Ca2+ regulates NHE1 activity.

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Language(s): eng - English
 Dates: 2011-09-062011-07-282011-09-192011-11-25
 Publication Status: Published in print
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1074/jbc.M111.286906
PMID: 21931166
PMC: PMC3220496
 Degree: -

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Title: The Journal of Biological Chemistry
  Other : JBC
  Abbreviation : J. Biol. Chem.
Source Genre: Journal
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Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 286 (47) Sequence Number: - Start / End Page: 40954 - 40961 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1