Immunohistochemical colocalization of TREK-1, TREK-2 and TRAAK with TRP channels in the trigeminal ganglion cells
Section snippets
Acknowledgements
This study was supported in part by a Grant-in-Aid from the JSPS, Japan (19380166).
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2019, NeuronCitation Excerpt :Surprisingly, this low level of identity does not preclude heteromerization, as we and others recently showed within the TREK subfamily (Blin et al., 2016; Hwang et al., 2014; Lengyel et al., 2016; Levitz et al., 2016). Based on this and the fact that TG neurons express many K2P channels (TREK1, TREK2, TRAAK, TASK1, and TASK3; Bautista et al., 2008; Yamamoto et al., 2009), we hypothesized that the difference between TRESK mutants is due to their differential ability to modify the function of other K2P channels through heteromerization. To assess the ability of TRESK to heteromerize with other K2P channels that are expressed in TG neurons, we used the single-molecule pull-down (“SiMPull”) assay (Jain et al., 2012) to visualize individual antibody-immobilized protein complexes on polyethylene-glycol-passivated glass coverslips (Figure 1A).