IndraLab

Statements


2 2 | 1 7

sparser
"In T-lymphocytes, PSD-95 interacts with Kv1.3, inducing clustering and recruiting Kv1.3 into the IS xref ."

sparser
"For example, PSD-95 interacts with Kv1.3 and favors its polarization toward the IS ( xref ), whereas the negative regulatory subunit KCNE4 interacts with Kv1.3 and retains the channel in the ER, impairing the channel targeting to the IS and therefore causing a reduction in T cell proliferation and IL-2 production ( xref )."

sparser
"Therefore, a functional Kv1.3-PSD-95 interaction is required not only for correct Kv1.3 redistribution in the vicinity of IS formation but also to prevent a massive internalization of the channel as a consequence of PKC-dependent immunosuppressive insults."

sparser
"Through patch-clamp electrophysiology, immunochemistry, and co-immunoprecipitation, we found that while Kv1.3 and PSD-95 alone interact via the canonical C-terminal PDZ recognition motif of the channel, this molecular site of interaction acts to cluster the channels but the PSD-95 SH(3)-guanylate kinase domain functionally modulates Kv1.3 activity via two proline-rich domains in its N- and C-terminal."

sparser
"In those cells, Dlg family members interacted with Kv1.3 channel protein and recruited Kv1.3 channel protein into the immunological synapse, protecting Kv1.3 channel protein from degradation."

reach
"In summary, PSD-95 binds to Src-family kinases and Kv1.3, favoring the phosphorylation of the channel [78]."

sparser
"PSD-95 associated with Kv1.3 in HEK-293 cells ( xref ), affecting the channel membrane distribution ( xref )."

sparser
"Kv1.3 interacts with PSD-95 through a C-terminal PDZ-binding domain, defined by the last three residues of the channel (Thr 523 -Asp 524 -Val 525 ) xref ."