Xenopus Pkdcc1 and Pkdcc2 are two new tyrosine kinases involved in the regulation of JNK dependent Wnt/PCP signaling pathway

Detalhes bibliográficos
Autor(a) principal: Belo, José
Data de Publicação: 2015
Outros Autores: Ramalho, José da Silva, Inácio, José Manuel Café
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10362/21491
Resumo: This work was supported by research grants from the Fundacao Ciencia e Tecnologia - IP (http://www.fct.pt/index.phtml.pt), and from IBB/CBME, LA to J. A. Belo in the frame of Projects ref degrees PTDC/BIA-BCM/69912/2006 and Pest-OE/EQB/LA0023/2013. M. Vitorino, A. C. Silva and J. M. Inacio are recipients of FCT post-doc fellowships.
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spelling Xenopus Pkdcc1 and Pkdcc2 are two new tyrosine kinases involved in the regulation of JNK dependent Wnt/PCP signaling pathwayANTERIOR PRIMITIVE ENDODERMVERTEBRATE GASTRULATIONWNTNEURAL-TUBE CLOSUREAPICAL CONSTRICTIONSECRETED FACTORPROTEINPLANAR CELL POLARITYCONVERGENT EXTENSIONPCP PATHWAYMultidisciplinary SciencesThis work was supported by research grants from the Fundacao Ciencia e Tecnologia - IP (http://www.fct.pt/index.phtml.pt), and from IBB/CBME, LA to J. A. Belo in the frame of Projects ref degrees PTDC/BIA-BCM/69912/2006 and Pest-OE/EQB/LA0023/2013. M. Vitorino, A. C. Silva and J. M. Inacio are recipients of FCT post-doc fellowships.Protein Kinase Domain Containing, Cytoplasmic (PKDCC) is a protein kinase which has been implicated in longitudinal bone growth through regulation of chondrocytes formation. Nevertheless, the mechanism by which this occurs remains unknown. Here, we identified two new members of the PKDCC family, Pkdcc1 and Pkdcc2 from Xenopus laevis. Interestingly, our knockdown experiments revealed that these two proteins are both involved on blastopore and neural tube closure during gastrula and neurula stages, respectively. In vertebrates, tissue polarity and cell movement observed during gastrulation and neural tube closure are controlled by Wnt/Planar Cell Polarity (PCP) molecular pathway. Our results showed that Pkdcc1 and Pkdcc2 promote the recruitment of Dvl to the plasma membrane. But surprisingly, they revealed different roles in the induction of a luciferase reporter under the control of Atf2 promoter. While Pkdcc1 induces Atf2 expression, Pkdcc2 does not, and furthermore inhibits its normal induction by Wnt11 and Wnt5a. Altogether our data show, for the first time, that members of the PKDCC family are involved in the regulation of JNK dependent Wnt/PCP signaling pathway.NOVA Medical School|Faculdade de Ciências Médicas (NMS|FCM)Centro de Estudos de Doenças Crónicas (CEDOC)RUNBelo, JoséRamalho, José da SilvaInácio, José Manuel Café2017-06-08T22:01:13Z2015-08-132015-08-13T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10362/21491eng1932-6203PURE: 488851https://doi.org/10.1371/journal.pone.0135504info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-03-11T04:08:13Zoai:run.unl.pt:10362/21491Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:26:49.287811Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Xenopus Pkdcc1 and Pkdcc2 are two new tyrosine kinases involved in the regulation of JNK dependent Wnt/PCP signaling pathway
title Xenopus Pkdcc1 and Pkdcc2 are two new tyrosine kinases involved in the regulation of JNK dependent Wnt/PCP signaling pathway
spellingShingle Xenopus Pkdcc1 and Pkdcc2 are two new tyrosine kinases involved in the regulation of JNK dependent Wnt/PCP signaling pathway
Belo, José
ANTERIOR PRIMITIVE ENDODERM
VERTEBRATE GASTRULATION
WNT
NEURAL-TUBE CLOSURE
APICAL CONSTRICTION
SECRETED FACTOR
PROTEIN
PLANAR CELL POLARITY
CONVERGENT EXTENSION
PCP PATHWAY
Multidisciplinary Sciences
title_short Xenopus Pkdcc1 and Pkdcc2 are two new tyrosine kinases involved in the regulation of JNK dependent Wnt/PCP signaling pathway
title_full Xenopus Pkdcc1 and Pkdcc2 are two new tyrosine kinases involved in the regulation of JNK dependent Wnt/PCP signaling pathway
title_fullStr Xenopus Pkdcc1 and Pkdcc2 are two new tyrosine kinases involved in the regulation of JNK dependent Wnt/PCP signaling pathway
title_full_unstemmed Xenopus Pkdcc1 and Pkdcc2 are two new tyrosine kinases involved in the regulation of JNK dependent Wnt/PCP signaling pathway
title_sort Xenopus Pkdcc1 and Pkdcc2 are two new tyrosine kinases involved in the regulation of JNK dependent Wnt/PCP signaling pathway
author Belo, José
author_facet Belo, José
Ramalho, José da Silva
Inácio, José Manuel Café
author_role author
author2 Ramalho, José da Silva
Inácio, José Manuel Café
author2_role author
author
dc.contributor.none.fl_str_mv NOVA Medical School|Faculdade de Ciências Médicas (NMS|FCM)
Centro de Estudos de Doenças Crónicas (CEDOC)
RUN
dc.contributor.author.fl_str_mv Belo, José
Ramalho, José da Silva
Inácio, José Manuel Café
dc.subject.por.fl_str_mv ANTERIOR PRIMITIVE ENDODERM
VERTEBRATE GASTRULATION
WNT
NEURAL-TUBE CLOSURE
APICAL CONSTRICTION
SECRETED FACTOR
PROTEIN
PLANAR CELL POLARITY
CONVERGENT EXTENSION
PCP PATHWAY
Multidisciplinary Sciences
topic ANTERIOR PRIMITIVE ENDODERM
VERTEBRATE GASTRULATION
WNT
NEURAL-TUBE CLOSURE
APICAL CONSTRICTION
SECRETED FACTOR
PROTEIN
PLANAR CELL POLARITY
CONVERGENT EXTENSION
PCP PATHWAY
Multidisciplinary Sciences
description This work was supported by research grants from the Fundacao Ciencia e Tecnologia - IP (http://www.fct.pt/index.phtml.pt), and from IBB/CBME, LA to J. A. Belo in the frame of Projects ref degrees PTDC/BIA-BCM/69912/2006 and Pest-OE/EQB/LA0023/2013. M. Vitorino, A. C. Silva and J. M. Inacio are recipients of FCT post-doc fellowships.
publishDate 2015
dc.date.none.fl_str_mv 2015-08-13
2015-08-13T00:00:00Z
2017-06-08T22:01:13Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10362/21491
url http://hdl.handle.net/10362/21491
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 1932-6203
PURE: 488851
https://doi.org/10.1371/journal.pone.0135504
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
institution RCAAP
reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
repository.mail.fl_str_mv
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