IndraLab

Statements

SLC5A3 binds KCNQ1. 20 / 20
| 1 19
sparser
"Here, SMIT1 had little to no effect on KCNQ1 voltage dependence or macroscopic current amplitude ( Fig. 4 , A – C ), although the resting membrane potential (RMP) of oocytes expressing KCNQ1-SMIT1 was[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
28793216
sparser
"This resulted in a 70% increase in KCNQ1-SMIT1 currents provoked by 1 μ M JNJ303, at −20 mV ( Fig. S13 E )."
28793216
sparser
"Our finding that co-assembly of SMIT1 with KCNQ1, KCNQ1/KCNE1, or KCNQ2/3 channels alters their ion selectivity strongly supports the idea that SMIT1 alters KCNQ pore conformation via close physical j[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
28793216
sparser
"Unexpectedly, JNJ303 was an agonist of KCNQ1-SMIT1, suggesting that SMIT1 may also bind to or affect the conformation of a site in S6 similar to that occupied by KCNE1."
28793216
reach
"KCNQ1 physically interacts with SMIT1 in the choroid plexus, in tripartite complexes with KCNE2, and in vitro is thought to also form complexes with the structurally related myo-inositol transporter, SMIT2 XREF_BIBR, XREF_BIBR."
32111967
sparser
"Thus, SMIT1 co-expression, in the absence of extracellular myo -inositol or other SMIT1 substrates, changes ion selectivity, voltage-dependence and pharmacology of KCNQ1 in a KCNE1-dependent manner, consistent with a model in which SMIT1 physically interacts with the KCNQ1 pore or close enough to it to alter its fundamental attributes."
28718502
sparser
"In vitro , SMIT1 can also form complexes with heterologously co-expressed KCNQ1, with or without KCNE2."
30959022
sparser
"In contrast, KCNQ1-SMIT1 had a G Rb / G K ratio of 3.0, reduced compared to homomeric KCNQ1 ( Fig. S10 , B and C , n = 18, p < 0.05), whereas KCNQ1-KCNE1-SMIT1 had a G Rb / G K ratio of 1.31, larger t[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
28793216
sparser
"However, the mean permeability of KCNQ1-SMIT1 for Cs + relative to K + was 0.42 ± 0.01 ( n = 10), compared to 0.26 ± 0.01 ( n = 7) for KCNQ1, a 61% increase in relative Cs + permeability ( Fig. S11 , [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
28793216
sparser
"SMIT1 also forms complexes with KCNQ1 when the two are heterologously co-expressed, and KCNE2 is not required for KCNQ1-SMIT1 complex assembly."
27789743
sparser
"KCNQ1 physically interacts with SMIT1 in the choroid plexus, in tripartite complexes with KCNE2, and in vitro is thought to also form complexes with the structurally related myo -inositol transporter, SMIT2 xref , xref ."
32111967
sparser
"This suggested close KCNQ-SMIT juxtaposition, an hypothesis supported by co-localization and/or co-immunoprecipitation of KCNQ1-SMIT1 and KCNQ2/3-SMIT1/2 complexes ( 10,11 )."
28793216
sparser
"Although currents generated by KCNQ1 or KCNQ1-SMIT1 were each attenuated compared to the value predicted from the GHK flux equation, SMIT1 presence was partially protective across the [K + ] o range e[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
28793216
sparser
"This reversed the polarity of the G / G max shifts exerted by TEA, from 11.3 mV more positive (KCNQ1 + TEA) to 13.2 mV more negative (KCNQ1-SMIT1 + TEA) ( Fig. 5 , A – D )."
28793216
sparser
"KCNQ1 can also form complexes with the Na + -coupled myo-inositol transporter SMIT1 (encoded by SLC5A3 )."
30443601
sparser
"Complex formation results in reciprocal regulation of both KCNQ1 and SMIT1, and KCNQ1-SMIT1 complexes in the choroid plexus epithelium are important for regulating cerebrospinal fluid myo-inositol content ( xref )."
30443601
sparser
"Here, MTX (30 μM) negative shifted the voltage dependence of KCNQ1-SMIT1 activation by a similar extent to effects on KCNQ1 alone ( xref , C to E, and fig."
30443601
sparser
"The potency and efficacy of MTX on KCNQ1-SMIT1 were similar to those for KCNQ1 ( xref )."
30443601
sparser
"KCNQ1-SMIT1 currents were likewise not inhibited by 1 μ M JNJ303, but, interestingly, instead exhibited a −8 mV shift in their voltage dependence of activation when exposed to 1 μ M JNJ303, compared t[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
28793216
sparser
"We previously showed that KCNQ1 forms complexes with SMIT1 in vivo and in vitro, but did not pursue a systematic examination of the effects of SMIT1 on KCNQ1 pore properties ( 10 )."
28793216