Unc5B interacts with FLRT3 and Rnd1 to modulate cell adhesion in Xenopus embryos.
The FLRT family of transmembrane proteins has been implicated in the regulation of FGF signalling, neurite outgrowth, homotypic cell sorting and cadherin-mediated adhesion. In an expression screen we identified the Netrin receptors Unc5B and Unc5D as high-affinity FLRT3 interactors. Upon overexpress...
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Format: | Article |
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Public Library of Science (PLoS)
2009-05-01
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Series: | PLoS ONE |
Online Access: | http://europepmc.org/articles/PMC2683942?pdf=render |
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author | Emil Karaulanov Ralph T Böttcher Peter Stannek Wei Wu Marlene Rau Souichi Ogata Ken W Y Cho Christof Niehrs |
author_facet | Emil Karaulanov Ralph T Böttcher Peter Stannek Wei Wu Marlene Rau Souichi Ogata Ken W Y Cho Christof Niehrs |
author_sort | Emil Karaulanov |
collection | DOAJ |
description | The FLRT family of transmembrane proteins has been implicated in the regulation of FGF signalling, neurite outgrowth, homotypic cell sorting and cadherin-mediated adhesion. In an expression screen we identified the Netrin receptors Unc5B and Unc5D as high-affinity FLRT3 interactors. Upon overexpression, Unc5B phenocopies FLRT3 and both proteins synergize in inducing cell deadhesion in Xenopus embryos. Morpholino knock-downs of Unc5B and FLRT3 synergistically affect Xenopus development and induce morphogenetic defects. The small GTPase Rnd1, which transmits FLRT3 deadhesion activity, physically and functionally interacts with Unc5B, and mediates its effect on cell adhesion. The results suggest that FLRT3, Unc5B and Rnd1 proteins interact to modulate cell adhesion in early Xenopus development. |
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issn | 1932-6203 |
language | English |
last_indexed | 2024-12-13T08:40:10Z |
publishDate | 2009-05-01 |
publisher | Public Library of Science (PLoS) |
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spelling | doaj.art-d7ef513c2d194a2b878e8d05fc99835a2022-12-21T23:53:34ZengPublic Library of Science (PLoS)PLoS ONE1932-62032009-05-0145e574210.1371/journal.pone.0005742Unc5B interacts with FLRT3 and Rnd1 to modulate cell adhesion in Xenopus embryos.Emil KaraulanovRalph T BöttcherPeter StannekWei WuMarlene RauSouichi OgataKen W Y ChoChristof NiehrsThe FLRT family of transmembrane proteins has been implicated in the regulation of FGF signalling, neurite outgrowth, homotypic cell sorting and cadherin-mediated adhesion. In an expression screen we identified the Netrin receptors Unc5B and Unc5D as high-affinity FLRT3 interactors. Upon overexpression, Unc5B phenocopies FLRT3 and both proteins synergize in inducing cell deadhesion in Xenopus embryos. Morpholino knock-downs of Unc5B and FLRT3 synergistically affect Xenopus development and induce morphogenetic defects. The small GTPase Rnd1, which transmits FLRT3 deadhesion activity, physically and functionally interacts with Unc5B, and mediates its effect on cell adhesion. The results suggest that FLRT3, Unc5B and Rnd1 proteins interact to modulate cell adhesion in early Xenopus development.http://europepmc.org/articles/PMC2683942?pdf=render |
spellingShingle | Emil Karaulanov Ralph T Böttcher Peter Stannek Wei Wu Marlene Rau Souichi Ogata Ken W Y Cho Christof Niehrs Unc5B interacts with FLRT3 and Rnd1 to modulate cell adhesion in Xenopus embryos. PLoS ONE |
title | Unc5B interacts with FLRT3 and Rnd1 to modulate cell adhesion in Xenopus embryos. |
title_full | Unc5B interacts with FLRT3 and Rnd1 to modulate cell adhesion in Xenopus embryos. |
title_fullStr | Unc5B interacts with FLRT3 and Rnd1 to modulate cell adhesion in Xenopus embryos. |
title_full_unstemmed | Unc5B interacts with FLRT3 and Rnd1 to modulate cell adhesion in Xenopus embryos. |
title_short | Unc5B interacts with FLRT3 and Rnd1 to modulate cell adhesion in Xenopus embryos. |
title_sort | unc5b interacts with flrt3 and rnd1 to modulate cell adhesion in xenopus embryos |
url | http://europepmc.org/articles/PMC2683942?pdf=render |
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