Kim, Seong-Seop Park, Jimin Kim, Eunju Hwang, Eun Mi Park, Jae-Yong 2024-01-19T09:31:03Z 2024-01-19T09:31:03Z 2023-06-29 2023-06 https://pubs.kist.re.kr/handle/201004/113657 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, beta-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, beta-COP binds to the C-terminus of TREK2 and reduces its cell surface expression but does not bind to TRAAK. Furthermore, beta-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 beta-COP in regulating the surface expression of the TREK family. English Multidisciplinary Digital Publishing Institute (MDPI) β-COP Suppresses the Surface Expression of the TREK2 Article 10.3390/cells12111500 1 Cells, v.12, no.11 Cells 12 11 Y scie scopus 001004702300001 2-s2.0-85161403288 Cell Biology Cell Biology Article K+ CHANNEL FUNCTIONAL HETERODIMERS POTASSIUM CHANNELS TRESK TRAFFICKING RETENTION TRANSPORT BINDING fi-COP protein-protein interaction TREK family TREK1 TREK2 TRAAK