IndraLab

Statements


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sparser
"Lacking its own palmitoylation, TREK-1 interacts with PLD2 through its unstructured C-terminus."

sparser
"PA appears to activate TREK-1 as phospholipase D2 (PLD2) directly binds to TREK-1 and activates the channel through local production of lipid ( xref )."

sparser
"Overall, the authors conclude that force is sensed by ordered lipids and PLD2 associates with TREK-1 to selectively gate the channel."

sparser
"PA and PG are both products of the enzyme PLD2 ( xref ), and we expect these lipids to agonize the channel as PLD2 binds directly to the C terminus of TREK-1 and activates the channel ( xref ) (see also xref )."

sparser
"Lastly, In our previous studies we showed activation of PLD2 by anesthetics was responsible for all of TREK-1’s anesthetic sensitivity and this was through PLD2 binding to the C-terminus of TREK-15."

reach
"The positive modulatory influences of anionic lipids and membrane tension appear to be mechanistically intertwined and both mechanical force and volatile anesthetics have been found to disrupt the association between TREK1 and PLD2 ."

reach
"In another example, PLD2 binds to TWIK-related potassium channel isotype 1 (TREK-1), producing local PA sufficient to activate the channel [67]."

reach
"Given that TREK-1 binds to PLD2, we hypothesized the channel could undergo a similar mechanically induced spatial reorganization between GM1 and PIP clusters."

sparser
"In addition to binding PIP 2 , PLD2 also binds directly to the C-terminus of TREK-1 and activates the channel through local production of phosphatidic acid [ xref , xref ], presumably in the disordered region of the cell membrane [ xref ]."

sparser
"Early TREK-1 studies[ xref , xref , xref ] were unaware of PLD2 mechano and anesthetic sensitivity [ xref , xref ] and the direct interaction of PLD2 with TREK-1[ xref ]."

sparser
"Also, the interaction of TREK-1 with PLD2 (producing PA) might differ in cells."

sparser
"First, mechanical force deforms the ordered lipids, which disrupts the interaction of PLD2 with the GM1 lipids and allows a complex of TREK-1 and PLD2 to associate with PIP 2 clusters."

sparser
"Intriguingly, the enzyme phospholipase D2 (PLD2) directly interacts with the C-terminus of TREK-1, activating the channel by locally producing phosphatidic acid (PA) ( xref )."

sparser
"This observation suggests that if the effect is through a specific PLD2-TREK-1 interaction, then removal of the PLD2 binding domain should also inhibit PLD2-evoked currents."