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Both IRBIT and long-IRBIT bind to and coordinately regulate Cl−/HCO3− exchanger AE2 activity through modulating the lysosomal degradation of AE2

Scientific reports, 2021-03, Vol.11 (1), p.5990-5990, Article 5990 [Peer Reviewed Journal]

The Author(s) 2021. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;The Author(s) 2021 ;ISSN: 2045-2322 ;EISSN: 2045-2322 ;DOI: 10.1038/s41598-021-85499-6 ;PMID: 33727633

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  • Title:
    Both IRBIT and long-IRBIT bind to and coordinately regulate Cl−/HCO3− exchanger AE2 activity through modulating the lysosomal degradation of AE2
  • Author: Itoh, Ryo ; Hatano, Naoya ; Murakami, Momoko ; Mitsumori, Kosuke ; Kawasaki, Satoko ; Wakagi, Tomoka ; Kanzaki, Yoshino ; Kojima, Hiroyuki ; Kawaai, Katsuhiro ; Mikoshiba, Katsuhiko ; Hamada, Koichi ; Mizutani, Akihiro
  • Subjects: Cell adhesion & migration ; Cell migration ; Cell size ; Gene expression ; Homeostasis ; Lysosomes ; mRNA
  • Is Part Of: Scientific reports, 2021-03, Vol.11 (1), p.5990-5990, Article 5990
  • Description: Abstract Anion exchanger 2 (AE2) plays crucial roles in regulating cell volume homeostasis and cell migration. We found that both IRBIT and Long-IRBIT (L-IRBIT) interact with anion exchanger 2 (AE2). The interaction occurred between the conserved AHCY-homologous domain of IRBIT/L-IRBIT and the N-terminal cytoplasmic region of AE2. Interestingly, AE2 activity was reduced in L-IRBIT KO cells, but not in IRBIT KO cells. Moreover, AE2 activity was slightly increased in IRBIT/L-IRBIT double KO cells. These changes in AE2 activity resulted from changes in the AE2 expression level of each mutant cell, and affected the regulatory volume increase and cell migration. The activity and expression level of AE2 in IRBIT/L-IRBIT double KO cells were downregulated if IRBIT, but not L-IRBIT, was expressed again in the cells, and the downregulation was cancelled by the co-expression of L-IRBIT. The mRNA levels of AE2 in each KO cell did not change, and the downregulation of AE2 in L-IRBIT KO cells was inhibited by bafilomycin A1. These results indicate that IRBIT binding facilitates the lysosomal degradation of AE2, which is inhibited by coexisting L-IRBIT, suggesting a novel regulatory mode of AE2 activity through the binding of two homologous proteins with opposing functions.
  • Publisher: London: Nature Publishing Group
  • Language: English
  • Identifier: ISSN: 2045-2322
    EISSN: 2045-2322
    DOI: 10.1038/s41598-021-85499-6
    PMID: 33727633
  • Source: PubMed Central
    ProQuest Central
    DOAJ Directory of Open Access Journals
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