Aquaporin-0-protein interactions elucidated by crosslinking mass spectrometry.

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  • Author(s): O'Neale CV;O'Neale CV; Tran MH; Tran MH; Schey KL; Schey KL
  • Source:
    Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2024 Oct 01; Vol. 727, pp. 150320. Date of Electronic Publication: 2024 Jun 27.
  • Publication Type:
    Journal Article; Research Support, N.I.H., Extramural
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Elsevier Country of Publication: United States NLM ID: 0372516 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1090-2104 (Electronic) Linking ISSN: 0006291X NLM ISO Abbreviation: Biochem Biophys Res Commun Subsets: MEDLINE
    • Publication Information:
      Publication: <2002- >: San Diego, CA : Elsevier
      Original Publication: New York, Academic Press.
    • Subject Terms:
      Aquaporins*/metabolism ; Aquaporins*/chemistry ; Eye Proteins*/metabolism ; Eye Proteins*/chemistry ; Mass Spectrometry*/methods ; Lens, Crystalline*/metabolism ; Lens, Crystalline*/chemistry ; Connexins*/metabolism ; Connexins*/chemistry; Animals ; Vimentin/metabolism ; Vimentin/chemistry ; Protein Binding ; Cross-Linking Reagents/chemistry ; Cross-Linking Reagents/metabolism ; alpha-Crystallins/metabolism ; alpha-Crystallins/chemistry
    • Abstract:
      Aquaporin-0 (AQP0) constitutes 50 % of the lens membrane proteome and plays important roles in lens fiber cell adhesion, water permeability, and lens transparency. Previous work has shown that specific proteins, such as calmodulin (CaM), interact with AQP0 to modulate its water permeability; however, these studies often used AQP0 peptides, rather than full-length protein, to probe these interactions. Furthermore, the specific regions of interaction of several known AQP0 interacting partners, i.e. αA and αB-crystallins, and phakinin (CP49) remain unknown. The purpose of this study was to use crosslinking mass spectrometry (XL-MS) to identify interacting proteins with full-length AQP0 in crude lens cortical membrane fractions and to determine the specific protein regions of interaction. Our results demonstrate, for the first time, that the AQP0 N-terminus can engage in protein interactions. Specific regions of interaction are elucidated for several AQP0 interacting partners including phakinin, α-crystallin, connexin-46, and connexin-50. In addition, two new interacting partners, vimentin and connexin-46, were identified.
      Competing Interests: Declaration of competing interest The authors declare the following financial interests/personal relationships which may be considered as potential competing interests:Kevin L. Schey reports financial support was provided by National Institutes of Health. Carla O'Neale reports financial support was provided by National Institutes of Health. If there are other authors, they declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
      (Copyright © 2024 The Authors. Published by Elsevier Inc. All rights reserved.)
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    • Grant Information:
      F31 EY032348 United States EY NEI NIH HHS; P30 EY008126 United States EY NEI NIH HHS; R01 EY013462 United States EY NEI NIH HHS; U01 AI150739 United States AI NIAID NIH HHS
    • Contributed Indexing:
      Keywords: Aquaporin-0; Crosslinking; Lens protein; Mass spectrometry; Membrane protein; Protein interaction
    • Accession Number:
      0 (Aquaporins)
      0 (aquaporin 0)
      0 (Eye Proteins)
      0 (Connexins)
      0 (connexin 50)
      0 (Vimentin)
      0 (Cross-Linking Reagents)
      0 (alpha-Crystallins)
    • Publication Date:
      Date Created: 20240704 Date Completed: 20240721 Latest Revision: 20241116
    • Publication Date:
      20241116
    • Accession Number:
      PMC11563185
    • Accession Number:
      10.1016/j.bbrc.2024.150320
    • Accession Number:
      38963984