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KCNMA1 binds CDC25. 9 / 9
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"Because we previously showed that the N-terminal region of CTN-1 interacts with DYB-1 [XREF_BIBR], these results indicate that CTN-1 can interact with SLO-1 and DYB-1."
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"Thus, we postulate that unlike CTN-1 DYB-1 is not necessary for the formation of macromolecular SLO-1 puncta, rather it stabilizes or maintains the SLO-1 and CTN-1 complex at the presynaptic terminals."
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"Moreover, CTN-1 is also similarly localized in unc-2 mutants, consistent with the direct interaction between CTN-1 and SLO-1."
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"Our data have now shown that the interaction between SLO-1 and CTN-1 requires both the RCK1 and RCK2 domains, raising the possibility that CTN-1 interacts with a patch on the outer surface of the RCK1 and RCK2 domains, as opposed to a stretch of amino acids within the two domains."
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"Previous studies by us and others showed that mutations in ctn-1, which displays extensive homology to both alpha-catenin and vinculin, suppress the sluggish movement of slo-1 gain-of-function mutants [XREF_BIBR], and that SLO-1 interacts with CTN-1 in C. elegans muscle and in heterologous cultured cells [XREF_BIBR]."
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"However, the physical and functional interaction between SLO-1 and CTN-1 in neurons has not been fully examined."
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"Based on the genetic interaction between ctn-1 and slo-1, and the observation that the integrity of the dystrophin complex and ISLO-1 localization are disrupted in ctn-1 mutants, we hypothesized that CTN-1 regulates the localization of SLO-1 in muscle."
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"Intriguingly, however, DYB-1 is not sufficient for tethering the SLO-1 and CTN-1 complex to presynaptic terminals."
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"Two cytoskeletal proteins, CTN-1 and DYB-1, are crucial for normal SLO-1 cluster formation; CTN-1 directly organizes SLO-1 clusters, and DYB-1 stabilizes or maintains the complex of CTN-1 and SLO-1 complex through the interaction with CTN-1."
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