IndraLab

"Bax binds to Kv1.3 and functionally inhibits mitochondrial Kv1.3 [ xref , xref ]."

"These studies showed that Bax inhibits Kv1.3 with an IC 50 in the low nM range whereas recombinant Bcl-2 or Bcl-x L were without effect."

"Since protonation of Histidine 404 of Kv1.3 has been shown to reduce the interaction of the pore with toxins, it is assumed that Bax binds to and inhibits Kv1.3 in a very similar manner as highly spec[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

"Wild-type Bax inhibited Kv1.3 activity in electrophysiological experiments, while BaxK128E mutant did not [33] ."

"We have previously shown that Kv1.3 is inhibited by Bax and contributes to a series of apoptotic events at the level of mitochondria (Szabò et al, xref ; Szabò et al, xref )."

"As we expected, Bax turned out to inhibit K V 1.3."

"Indeed, tBid initiates a CsA-sensitive process of cristae remodeling that increases cytochrome c availability in the intermembrane space, which is consistent with a PT-dependent facilitation of cytochrome c release even when the outer membrane is intact (Scorrano et al., xref , xref ); and Bax inhibits the mitochondrial inner membrane potassium channel Kv1.3 (Szabó et al., xref ), a proapoptotic effect that critically depends on Bax residue K128 and is abrogated by a K128E mutation, while an E158K mutation in antiapoptotic Bcl-xL (position 158 of Bcl-xL corresponds to position 128 of Bax) turns Bcl-xL into a proapoptotic protein (Szabó et al., xref )."

"This work demonstrated that in lymphocytes Bax physically interacts with and inhibits Kv1.3 channels causing hyperpolarization and then overproduction of ROS, which eventually causes PTP opening, stab[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

"The amino acid residue K128 in Bax seems indeed to be particularly important for the interaction of Bax with mtK V 1.3, since mutation of this lysine to glutamic acid abrogated inhibition of K V 1.3 b[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

"Intriguingly, Bax physically interacts with mitoKv1.3 in apoptotic cells, significantly inhibiting Kv1.3 activity at nanomolar concentrations of Bax (Leanza et al. 2012, Szabó et al. 2008)."

"These studies showed that Bax inhibits Kv1.3 with an IC 50 in the low nM range whereas recombinant Bcl-2 or Bcl-x L were without effect."