IndraLab

Statements

KCNMA1 binds CTNNB1. 42 / 48
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"To study β-catenin-HSlo interactions we used an HSlo-HEK stable cell line, and ascertained the distribution of HSlo on the surface of these cells."
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"This pattern of staining was reminiscent of cell adhesion complexes, and suggested that this cell line could serve as a model system to study interactions between HSlo and β-catenin."
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"We tested the binding between beta-catenin and HSlo by purifying HSlo tagged with the FLAG epitope."
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"One possible explanation for the seemingly incongruent data is that HSlo interacts with β-catenin in regions outside the S10 region."
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"In yeast two-hybrid experiments xref it was shown that the interaction between Slo and β-catenin was limited to the S10 region."
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"These four peptides were used in an in vitro competitive binding assay to test the efficacy of HSlo binding to β-catenin."
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"As shown in xref , the peptide beginning at residue E562 has significant inhibitory effects on HSlo binding to β-catenin."
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"Alongside the effects on surface expression of Slo channel, we also have evidence that the interaction between β-catenin and Slo may stabilize the Slo channel and protect it from proteolytic degradation."
22194818
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"This may be due to loss of protection conferred by β-catenin binding to HSlo, causing the mutant channel protein become less stable and more prone to proteolytic degradation."
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"Together, these results are consistent with a stable interaction between beta -catenin and HSlo."
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"This would argue for a stable interaction between beta-catenin and HSlo that is partially dependent on the participation of amino acids in the S10 region of HSlo."
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"Our data show that the interaction between beta-catenin and Hslo affects channel surface expression, and that mutations of putative GSK phosphorylation sites in the S10 interaction domain in HSlo change both surface expression and channel kinetics."
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"Thus, these authors established that Slo and β-catenin were associated, although the physiological significance of this interaction was unclear."
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"Since both beta-catenin and GSK are involved in the canonical Wnt pathway XREF_BIBR, we speculate that the interaction between beta-catenin and HSlo may also affect Wnt signaling."
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"The fact that the S10 deletion mutant and two phosphorylation mutants behave similarly to wild type HSlo in inhibiting Wnt signaling points to the possibility of multiple modes of interaction between HSlo and beta-catenin."
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"While they were able to demonstrate interactions between Slo and β-catenin in vivo by pull-down assays, they were unable to demonstrate a direct interaction between these proteins by heterologous expression in COS cells xref ."
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"We demonstrate that the interaction between Slo and β-catenin is important for Slo surface expression in HEK-293 cells and chick hair cells in culture."
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"These four peptides were used in an in vitro competitive binding assay to test the efficacy of HSlo binding to beta-catenin."
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"As shown in XREF_FIG, the peptide beginning at residue E562 has significant inhibitory effects on HSlo binding to beta-catenin."
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"Irrespective of the exact mechanisms that underlie these phenomena that must await future exploration, these data point to a complex and dynamic interaction between HSlo and beta-catenin."
22194818
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"The complex behavior of HSlo mutants in TOP-FLASH assays indicates a complexity in HSlo interaction with β-catenin."
22194818
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"The fact that the S10 deletion mutant and two phosphorylation mutants behave similarly to wild type HSlo in inhibiting Wnt signaling points to the possibility of multiple modes of interaction between HSlo and β-catenin."
22194818
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"Alongside the effects on surface expression of Slo channel, we also have evidence that the interaction between beta-catenin and Slo may stabilize the Slo channel and protect it from proteolytic degradation."
22194818
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"This may be due to loss of protection conferred by beta-catenin binding to HSlo, causing the mutant channel protein become less stable and more prone to proteolytic degradation."
22194818
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"This possibility was confirmed by β-catenin binding to multiple Hslo peptides in a peptide array."
22194818
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"Similarly, while our data show clear physiological effects of HSlo interactions with β-catenin on the one hand increasing HSlo surface expression and on the other hand decreasing Wnt signaling, we do not have a satisfactory explanation for the seeming discordance between the observed physiological effects of the interaction between these proteins and their physical interaction."
22194818
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"Irrespective of the exact mechanisms that underlie these phenomena that must await future exploration, these data point to a complex and dynamic interaction between HSlo and β-catenin."
22194818
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"This effect is likely due to HSlo interactions with β-catenin, which may in turn reduce the size of the free pool of β-catenin available for activating Wnt signaling."
22194818
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"Since the S10 region is important for surface expression and since interaction of HSlo with β-catenin was thought to be mediated by the S10 region, we hypothesized that β-catenin was important for the surface expression of Slo through its interaction with Slo at the S10 region."
22194818
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"We were able to demonstrate direct binding of highly purified β-catenin (99%) and peptide fragments of HSlo."
22194818
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"The initial rationale that led to the detection of interactions between Slo and β-catenin was to ascertain mechanisms that led to Slo localization at the basolateral surface of hair cells (along with voltage gated Ca 2+ channels)."
22194818
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"The data presented up to this point clearly show the interaction between β-catenin and HSlo in the S10 region of HSlo is important for channel surface expression, and possibly also affecting channel stability."
22194818
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"This would argue for a stable interaction between β-catenin and HSlo that is partially dependent on the participation of amino acids in the S10 region of HSlo."
22194818
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"Our co-IP data indicates that the mechanism of the interaction of HSlo with β-catenin through the S10 region and its significance in HSlo surface expression may lie in a simple binding between these two proteins."
22194818
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"Since the association was not completely lost with HSloΔS10 in co-IP experiments, the possibility is raised that HSlo interactions with β-catenin may extend to regions outside the S10 region."
22194818
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"Our data show that the interaction between β-catenin and Hslo affects channel surface expression, and that mutations of putative GSK phosphorylation sites in the S10 interaction domain in HSlo change both surface expression and channel kinetics."
22194818
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"Indeed, our HSlo peptide array experiments identified 10 more sites on HSlo that potentially binds to β-catenin."
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"Furthermore, our in vitro competitive binding experiments confirm that at least one of the possible sites outside S10, namely the 38 residue sequence beginning at residue E562, significantly reduces HSlo binding to immobilized β-catenin."
22194818
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"Since both β-catenin and GSK are involved in the canonical Wnt pathway xref , we speculate that the interaction between β-catenin and HSlo may also affect Wnt signaling."
22194818
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"We demonstrate that the interaction between Slo and beta-catenin is important for Slo surface expression in HEK-293 cells and chick hair cells in culture."
22194818
reach
"This pattern of staining was reminiscent of cell adhesion complexes, and suggested that this cell line could serve as a model system to study interactions between HSlo and beta-catenin."
22194818
reach
"The initial rationale that led to the detection of interactions between Slo and beta-catenin was to ascertain mechanisms that led to Slo localization at the basolateral surface of hair cells (along with voltage gated Ca 2+ channels)."
22194818