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The E3 ubiquitin ligase Hace1 is required for early embryonic development in Xenopus laevis

BACKGROUND: HECT domain and ankyrin repeat containing E3 ubiquitin protein ligase 1 (HACE1) regulates a wide variety of cellular processes. It has been shown that one of the targets of HACE1 is the GTP-bound form of the small GTPase Rac1. However, the role of HACE1 in early development remains unkno...

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Autores principales: Iimura, Akira, Yamazaki, Fuhito, Suzuki, Toshiyasu, Endo, Tatsuya, Nishida, Eisuke, Kusakabe, Morioh
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5031333/
https://www.ncbi.nlm.nih.gov/pubmed/27653971
http://dx.doi.org/10.1186/s12861-016-0132-y
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author Iimura, Akira
Yamazaki, Fuhito
Suzuki, Toshiyasu
Endo, Tatsuya
Nishida, Eisuke
Kusakabe, Morioh
author_facet Iimura, Akira
Yamazaki, Fuhito
Suzuki, Toshiyasu
Endo, Tatsuya
Nishida, Eisuke
Kusakabe, Morioh
author_sort Iimura, Akira
collection PubMed
description BACKGROUND: HECT domain and ankyrin repeat containing E3 ubiquitin protein ligase 1 (HACE1) regulates a wide variety of cellular processes. It has been shown that one of the targets of HACE1 is the GTP-bound form of the small GTPase Rac1. However, the role of HACE1 in early development remains unknown. RESULTS: In situ hybridization revealed that Xenopus laevis hace1 is specifically expressed in the ectoderm at the blastula and gastrula stages and in the epidermis, branchial arch, kidney, and central nervous system at the tailbud stage. Knockdown of hace1 in Xenopus laevis embryos via antisense morpholino oligonucleotides led to defects in body axis elongation, pigment formation, and eye formation at the tadpole stage. Experiments with Keller sandwich explants showed that hace1 knockdown inhibited convergent extension, a morphogenetic movement known to be crucial for body axis elongation. In addition, time lapse imaging of whole embryos during the neurula stage indicated that hace1 knockdown also delayed neural tube closure. The defects caused by hace1 knockdown were partly rescued by knockdown of rac1. Moreover, embryos expressing a constitutively active form of Rac1 displayed phenotypes similar to those of embryos with hace1 knocked down. CONCLUSIONS: Our results suggest that Xenopus laevis hace1 plays an important role in early embryonic development, possibly via regulation of Rac1 activity. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12861-016-0132-y) contains supplementary material, which is available to authorized users.
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spelling pubmed-50313332016-09-29 The E3 ubiquitin ligase Hace1 is required for early embryonic development in Xenopus laevis Iimura, Akira Yamazaki, Fuhito Suzuki, Toshiyasu Endo, Tatsuya Nishida, Eisuke Kusakabe, Morioh BMC Dev Biol Research Article BACKGROUND: HECT domain and ankyrin repeat containing E3 ubiquitin protein ligase 1 (HACE1) regulates a wide variety of cellular processes. It has been shown that one of the targets of HACE1 is the GTP-bound form of the small GTPase Rac1. However, the role of HACE1 in early development remains unknown. RESULTS: In situ hybridization revealed that Xenopus laevis hace1 is specifically expressed in the ectoderm at the blastula and gastrula stages and in the epidermis, branchial arch, kidney, and central nervous system at the tailbud stage. Knockdown of hace1 in Xenopus laevis embryos via antisense morpholino oligonucleotides led to defects in body axis elongation, pigment formation, and eye formation at the tadpole stage. Experiments with Keller sandwich explants showed that hace1 knockdown inhibited convergent extension, a morphogenetic movement known to be crucial for body axis elongation. In addition, time lapse imaging of whole embryos during the neurula stage indicated that hace1 knockdown also delayed neural tube closure. The defects caused by hace1 knockdown were partly rescued by knockdown of rac1. Moreover, embryos expressing a constitutively active form of Rac1 displayed phenotypes similar to those of embryos with hace1 knocked down. CONCLUSIONS: Our results suggest that Xenopus laevis hace1 plays an important role in early embryonic development, possibly via regulation of Rac1 activity. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12861-016-0132-y) contains supplementary material, which is available to authorized users. BioMed Central 2016-09-21 /pmc/articles/PMC5031333/ /pubmed/27653971 http://dx.doi.org/10.1186/s12861-016-0132-y Text en © The Author(s). 2016 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Research Article
Iimura, Akira
Yamazaki, Fuhito
Suzuki, Toshiyasu
Endo, Tatsuya
Nishida, Eisuke
Kusakabe, Morioh
The E3 ubiquitin ligase Hace1 is required for early embryonic development in Xenopus laevis
title The E3 ubiquitin ligase Hace1 is required for early embryonic development in Xenopus laevis
title_full The E3 ubiquitin ligase Hace1 is required for early embryonic development in Xenopus laevis
title_fullStr The E3 ubiquitin ligase Hace1 is required for early embryonic development in Xenopus laevis
title_full_unstemmed The E3 ubiquitin ligase Hace1 is required for early embryonic development in Xenopus laevis
title_short The E3 ubiquitin ligase Hace1 is required for early embryonic development in Xenopus laevis
title_sort e3 ubiquitin ligase hace1 is required for early embryonic development in xenopus laevis
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5031333/
https://www.ncbi.nlm.nih.gov/pubmed/27653971
http://dx.doi.org/10.1186/s12861-016-0132-y
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