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http://purl.uniprot.org/citations/17916086http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17916086http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17916086http://www.w3.org/2000/01/rdf-schema#comment"The small G protein Rap1 regulates diverse cellular processes such as integrin activation, cell adhesion, cell-cell junction formation and cell polarity. It is crucial to identify Rap1 effectors to better understand the signalling pathways controlling these processes. Krev interaction trapped 1 (Krit1), a protein with FERM (band four-point-one/ezrin/radixin/moesin) domain, was identified as a Rap1 partner in a yeast two-hybrid screen, but this interaction was not confirmed in subsequent studies. As the evidence suggests a role for Krit1 in Rap1-dependent pathways, we readdressed this question. In the present study, we demonstrate by biochemical assays that Krit1 interacts with Rap1A, preferentially its GTP-bound form. We show that, like other FERM proteins, Krit1 adopts two conformations: a closed conformation in which its N-terminal NPAY motif interacts with its C-terminus and an opened conformation bound to integrin cytoplasmic domain associated protein (ICAP)-1, a negative regulator of focal adhesion assembly. We show that a ternary complex can form in vitro between Krit1, Rap1 and ICAP-1 and that Rap1 binds the Krit1 FERM domain in both closed and opened conformations. Unlike ICAP-1, Rap1 does not open Krit1. Using sedimentation assays, we show that Krit1 binds in vitro to microtubules through its N- and C-termini and that Rap1 and ICAP-1 inhibit Krit1 binding to microtubules. Consistently, YFP-Krit1 localizes on cyan fluorescent protein-labelled microtubules in baby hamster kidney cells and is delocalized from microtubules upon coexpression with activated Rap1V12. Finally, we show that Krit1 binds to phosphatidylinositol 4,5-P(2)-containing liposomes and that Rap1 enhances this binding. Based on these results, we propose a model in which Krit1 would be delivered by microtubules to the plasma membrane where it would be captured by Rap1 and ICAP-1."xsd:string
http://purl.uniprot.org/citations/17916086http://purl.org/dc/terms/identifier"doi:10.1111/j.1742-4658.2007.06068.x"xsd:string
http://purl.uniprot.org/citations/17916086http://purl.org/dc/terms/identifier"doi:10.1111/j.1742-4658.2007.06068.x"xsd:string
http://purl.uniprot.org/citations/17916086http://purl.uniprot.org/core/author"Beraud-Dufour S."xsd:string
http://purl.uniprot.org/citations/17916086http://purl.uniprot.org/core/author"Beraud-Dufour S."xsd:string
http://purl.uniprot.org/citations/17916086http://purl.uniprot.org/core/author"Chardin P."xsd:string
http://purl.uniprot.org/citations/17916086http://purl.uniprot.org/core/author"Chardin P."xsd:string
http://purl.uniprot.org/citations/17916086http://purl.uniprot.org/core/author"Albiges-Rizo C."xsd:string
http://purl.uniprot.org/citations/17916086http://purl.uniprot.org/core/author"Albiges-Rizo C."xsd:string
http://purl.uniprot.org/citations/17916086http://purl.uniprot.org/core/author"Gautier R."xsd:string
http://purl.uniprot.org/citations/17916086http://purl.uniprot.org/core/author"Gautier R."xsd:string
http://purl.uniprot.org/citations/17916086http://purl.uniprot.org/core/author"Faurobert E."xsd:string
http://purl.uniprot.org/citations/17916086http://purl.uniprot.org/core/author"Faurobert E."xsd:string
http://purl.uniprot.org/citations/17916086http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17916086http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17916086http://purl.uniprot.org/core/name"FEBS J."xsd:string
http://purl.uniprot.org/citations/17916086http://purl.uniprot.org/core/name"FEBS J."xsd:string
http://purl.uniprot.org/citations/17916086http://purl.uniprot.org/core/pages"5518-5532"xsd:string
http://purl.uniprot.org/citations/17916086http://purl.uniprot.org/core/pages"5518-5532"xsd:string
http://purl.uniprot.org/citations/17916086http://purl.uniprot.org/core/title"Krit 1 interactions with microtubules and membranes are regulated by Rap1 and integrin cytoplasmic domain associated protein-1."xsd:string
http://purl.uniprot.org/citations/17916086http://purl.uniprot.org/core/title"Krit 1 interactions with microtubules and membranes are regulated by Rap1 and integrin cytoplasmic domain associated protein-1."xsd:string
http://purl.uniprot.org/citations/17916086http://purl.uniprot.org/core/volume"274"xsd:string
http://purl.uniprot.org/citations/17916086http://purl.uniprot.org/core/volume"274"xsd:string
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