2019
DOI: 10.1016/j.celrep.2019.01.097
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Kibra Modulates Learning and Memory via Binding to Dendrin

Abstract: Highlights d Kibra WW tandem domains bind to Dendrin with lownanomolar affinity d Structure of Kibra WW domains bound to Dendrin PY motifs reveals the binding mechanism d Disruption of the Kibra/Dendrin interaction impairs learning and memory in mice d A Kibra mutation associated with Tourette syndrome causes defects in Dendrin binding

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Cited by 37 publications
(90 citation statements)
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“…Notably, the extensive interactions between the inter-domain linker and the C-terminal helix stabilize the supramodular structure of the MAGI2 WW tandem, and the Dendrin PY23 binds to the MAGI2 WW tandem following almost the exactly same detailed interactions as those observed in the KIBRA WW12/Dendrin PY23 complex ( Fig. 3E) (Ji et al, 2019).…”
Section: The Ww Tandems Of Magi2/3 and Kibra Resemble With Each Othermentioning
confidence: 73%
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“…Notably, the extensive interactions between the inter-domain linker and the C-terminal helix stabilize the supramodular structure of the MAGI2 WW tandem, and the Dendrin PY23 binds to the MAGI2 WW tandem following almost the exactly same detailed interactions as those observed in the KIBRA WW12/Dendrin PY23 complex ( Fig. 3E) (Ji et al, 2019).…”
Section: The Ww Tandems Of Magi2/3 and Kibra Resemble With Each Othermentioning
confidence: 73%
“…We have also demonstrated that bindings of short PY motif containing peptides to WW tandems can be readily enhanced to sub-nanomolar affinities (Fig. 6B), and these super-strong WW tandem binding peptides may be used as effective tools for studying the role of specific interactions between WW tandem proteins and target proteins (see (Ji et al, 2019) for an example). As for the very weak WW domain/target interactions, cautions are required in interpreting potential functional implications of such bindings.…”
Section: Discussionmentioning
confidence: 87%
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