IndraLab

Statements


4 | 20

sparser
"Multiple lines of evidence suggest that the interaction between Kv1.3 and Cav1 in mitochondria prevents Kv1.3 mediated cell-death."

sparser
"The Kv1.3 interaction with Cav1 can drive the channel either to the membrane and support proliferation or to mitochondria."

No evidence text available

sparser
"We have previously described that the interaction between Kv1.3 and Cav1 results in the localization of the channel to lipid rafts and caveolae ( xref ; xref )."

sparser
"By using a caveolin association-deficient channel (Kv1.3 CDB less ), we demonstrate here that while the Kv1.3-Cav1 interaction is responsible for the channel localization in the plasma membrane, a lack of such interaction accumulates Kv1.3 in the mitochondria."

sparser
"As mentioned above, the lack of interaction between Kv1.3 CBD less and Cav1 drastically impaired the cell surface targeting of the channel."

sparser
"Such an effect would justify the proposal of a Cav1-Kv1.3 axis, and would be a very relevant finding adding to the emerging importance of both Cav1 and Kv1.3 in physiology and pathology, especially in cancer."

sparser
"In an earlier paper (Sci Rep 2016;6:22453), the authors reported that the CBDless Kv1.3 mutant did not interact with caveolin-1 and exhibited reduced lipid raft portioning."

sparser
"By using a caveolin association-deficient channel (Kv1.3 CBD less ), we demonstrate here that while the Kv1.3Cav1 interaction is responsible for the channel localization in the plasma membrane, a lack of such interaction accumulates Kv1.3 in the mitochondria."

sparser
"The sequence for the CBD (ɸxxxxɸxxɸ, where ɸ is an aromatic residue and x is an unspecified amino acid) of Kv1.3 is F QRQV W LL F . To further study the nature of the Kv1.3Cav1 interaction, we abrogated the CBD by replacing the aromatic residues with Ala or Gly (Kv1.3 CBD less , xref )."

sparser
"To understand the mechanisms that contribute to these seemingly opposing roles of Kv1.3, this study examines the contribution of interaction between caveolin 1 (Cav1) and Kv1.3 channels on subcellular distribution and functional properties."

sparser
"Capera et al. cover an interesting topic in their manuscript, which reports a novel role of the interaction between caveolin 1 and Kv1.3 channels."

sparser
"Because the Kv1.3 and Cav1 interaction in lipid rafts has an enormous influence on cell physiology ( xref ; xref ; xref ), we analyzed the functional link between Kv1.3 and Cav1 in the regulation of intrinsic apoptosis."

No evidence text available

sparser
"The main conclusion of the paper is that the interaction between Kv1.3 and Cav1 plays a crucial role not only in the proper plasma membrane localization of Kv1.3, resulting in an enrichment of mitochondrial localization, but that the interaction with Cav1 at the mitochondria also modulates the induction of apoptosis."

sparser
"Here the data show that prevention of Cav1 binding to Kv1.3 channels results in a drastic change."

sparser
"We demonstrated that the interaction of Kv1.3 with Cav1 is important for the plasma membrane targeting of the channel."

sparser
"• If Kv1.3's association with caveolin-1 is essential to localize Kv1.3 in lipid raft membrane microdomains in the plasma membrane, how do Kv1.3 channels in caveolin-1 deficient Jurkat cells translocate to the plasma membrane and generate normal Kv1.3 currents (J Biol Chem."

sparser
"Deletion of the CBD motif of Kv1.3 caused the loss of Kv1.3Cav1 association, as demonstrated by the absence of co-IP and Förster resonance energy transfer (FRET) ( xref )."

No evidence text available

sparser
"Authors concluded that Kv1.3-caveolin 1 "crosstalk" can sensitize the cancer cells to apoptosis."

sparser
"MitoKv1.3 sensitizes cells to apoptosis, in agreement with our previous observation ( xref ), and possibly, mitochondrial Kv1.3 interaction with Cav1 modulates the pro-apoptotic effects of the channel."

No evidence text available

sparser
"Our results indicate that the interaction of Kv1.3 with Cav1 has important physiological consequences for controlling apoptosis."