IndraLab

Statements


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sparser
"We show, through GST pull-down assays and co-immunoprecipitation, that Kv4.3 protein associates with c-Src and that the SH2 and SH3 domains of the kinase mediate this interaction."

sparser
"Having confirmed an interaction between Kv4.3 and c-Src ( Fig. 2 ), we next sought to determine whether Kv4.3 channels could be tyrosine phosphorylated."

sparser
"In the present study we used an HEK293 cell line expressing Kv4.3 and provide evidence, for the first time, that Kv4.3 physically interacts with c-Src and that this interaction has the functional cons[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

reach
"The results presented here suggest that c-Src interaction and/or phosphorylation of Kv4.3 channels translates into an effect on current amplitude, and does not seem to affect voltage dependence and ki[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"We first examined whether Kv4.3 could interact with c-Src by performing an in vitro binding assay using GST fusion proteins with the Src SH2 and SH3 domains (GST-Src-SH2 and GST-Src-SH3)."

sparser
"To determine whether Kv4.3-c-Src complexes also occur in intact cells, we performed co-immunoprecipitation studies in lysates from HEK293-Kv4.3 cells with endogenous or overexpressed c-Src ( Fig. 2 C,[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"Our work presents evidence supporting a direct physical interaction between c-Src and Kv4.3 channels."

sparser
"Because physical interactions between Src kinases and their substrates are critical for efficient target phosphorylation [38,39] , the interaction between Kv4.3 and c-Src may also contribute to the ra[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"Because the Kv4.3-c-Src complex resides in the plasma membrane it is appropriately positioned to receive, and respond to, extracellular signals."

reach
"We show, through GST pull-down assays and co-immunoprecipitation, that Kv4.3 protein associates with c-Src and that the SH2 and SH3 domains of the kinase mediate this interaction."

reach
"Pull-down experiments performed on lysates prepared from HEK293-Kv4.3 cells showed that Kv4.3 is efficiently precipitated by both GST-Src-SH2 and GST-Src-SH3 but not by GST alone ( Fig. 2 B) strongly [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

reach
"Having confirmed an interaction between Kv4.3 and c-Src ( Fig. 2 ), we next sought to determine whether Kv4.3 channels could be tyrosine phosphorylated."

reach
"Because physical interactions between Src kinases and their substrates are critical for efficient target phosphorylation [38,39] , the interaction between Kv4.3 and c-Src may also contribute to the ra[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"