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Detection of Heterodimerization of Protein Isoforms Using an in Situ Proximity Ligation Assay
Published on: October 20, 2018
Emerging Roles of TWIK-1 Heterodimerization in the Brain
Chang-Hoon Cho1, Eun Mi Hwang2,3, Jae-Yong Park4
1School of Biosystem and Biomedical Science, College of Health Science, Korea University, Seoul 136-703, Korea. chois007@korea.ac.kr.
Abstract:
Two-pore domain K⁺ (K2P) channels play essential roles in regulating resting membrane potential and cellular excitability. Although TWIK-1 (TWIK-tandem of pore domains in a weak inward rectifying K⁺ channel) was the first identified member of the K2P channel family, it is only in recent years that the physiological roles of TWIK-1 have been studied in depth. A series of reports suggest that TWIK-1 may underlie diverse functions, such as intrinsic excitability of neurons, astrocytic passive conductance, and astrocytic glutamate release, as a homodimer or heterodimer with other K2P isotypes. Here, we summarize expression patterns and newly identified functions of TWIK-1 in the brain.
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