β-COP Suppresses the Surface Expression of the TREK2

Seong Seop Kim, Jimin Park, Eunju Kim, Eun Mi Hwang, Jae Yong Park

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)

Abstract

K2P channels, also known as two-pore domain K+ channels, play a crucial role in maintaining the cell membrane potential and contributing to potassium homeostasis due to their leaky nature. The TREK, or tandem of pore domains in a weak inward rectifying K+ channel (TWIK)-related K+ channel, subfamily within the K2P family consists of mechanical channels regulated by various stimuli and binding proteins. Although TREK1 and TREK2 within the TREK subfamily share many similarities, β-COP, which was previously known to bind to TREK1, exhibits a distinct binding pattern to other members of the TREK subfamily, including TREK2 and the TRAAK (TWIK-related acid-arachidonic activated K+ channel). In contrast to TREK1, β-COP binds to the C-terminus of TREK2 and reduces its cell surface expression but does not bind to TRAAK. Furthermore, β-COP cannot bind to TREK2 mutants with deletions or point mutations in the C-terminus and does not affect the surface expression of these TREK2 mutants. These results emphasize the unique role of β-COP in regulating the surface expression of the TREK family.

Original languageEnglish
Article number1500
JournalCells
Volume12
Issue number11
DOIs
Publication statusPublished - 2023 Jun

Bibliographical note

Publisher Copyright:
© 2023 by the authors.

Keywords

  • TRAAK
  • TREK family
  • TREK1
  • TREK2
  • protein-protein interaction
  • β-COP

ASJC Scopus subject areas

  • General Biochemistry,Genetics and Molecular Biology

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