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Identification of Sumoylated Proteins in the Silkworm Bombyx mori

Small ubiquitin-like modifier (SUMO) modification (SUMOylation) is an important and widely used reversible modification system in eukaryotic cells. It regulates various cell processes, including protein targeting, transcriptional regulation, signal transduction, and cell division. To understand its...

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Autores principales: Tang, Xudong, Fu, Xuliang, Hao, Bifang, Zhu, Feng, Xiao, Shengyan, Xu, Li, Shen, Zhongyuan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4284691/
https://www.ncbi.nlm.nih.gov/pubmed/25470021
http://dx.doi.org/10.3390/ijms151222011
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author Tang, Xudong
Fu, Xuliang
Hao, Bifang
Zhu, Feng
Xiao, Shengyan
Xu, Li
Shen, Zhongyuan
author_facet Tang, Xudong
Fu, Xuliang
Hao, Bifang
Zhu, Feng
Xiao, Shengyan
Xu, Li
Shen, Zhongyuan
author_sort Tang, Xudong
collection PubMed
description Small ubiquitin-like modifier (SUMO) modification (SUMOylation) is an important and widely used reversible modification system in eukaryotic cells. It regulates various cell processes, including protein targeting, transcriptional regulation, signal transduction, and cell division. To understand its role in the model lepidoptera insect Bombyx mori, a recombinant baculovirus was constructed to express an enhanced green fluorescent protein (eGFP)-SUMO fusion protein along with ubiquitin carrier protein 9 of Bombyx mori (BmUBC9). SUMOylation substrates from Bombyx mori cells infected with this baculovirus were isolated by immunoprecipitation and identified by LC–ESI-MS/MS. A total of 68 candidate SUMOylated proteins were identified, of which 59 proteins were functionally categorized to gene ontology (GO) terms. Analysis of kyoto encyclopedia of genes and genomes (KEGG) pathways showed that 46 of the identified proteins were involved in 76 pathways that mainly play a role in metabolism, spliceosome and ribosome functions, and in RNA transport. Furthermore, SUMOylation of four candidates (polyubiquitin-C-like isoform X1, 3-hydroxyacyl-CoA dehydrogenase, cyclin-related protein FAM58A-like and GTP-binding nuclear protein Ran) were verified by co-immunoprecipitation in Drosophila schneide 2 cells. In addition, 74% of the identified proteins were predicted to have at least one SUMOylation site. The data presented here shed light on the crucial process of protein sumoylation in Bombyx mori.
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spelling pubmed-42846912015-01-21 Identification of Sumoylated Proteins in the Silkworm Bombyx mori Tang, Xudong Fu, Xuliang Hao, Bifang Zhu, Feng Xiao, Shengyan Xu, Li Shen, Zhongyuan Int J Mol Sci Article Small ubiquitin-like modifier (SUMO) modification (SUMOylation) is an important and widely used reversible modification system in eukaryotic cells. It regulates various cell processes, including protein targeting, transcriptional regulation, signal transduction, and cell division. To understand its role in the model lepidoptera insect Bombyx mori, a recombinant baculovirus was constructed to express an enhanced green fluorescent protein (eGFP)-SUMO fusion protein along with ubiquitin carrier protein 9 of Bombyx mori (BmUBC9). SUMOylation substrates from Bombyx mori cells infected with this baculovirus were isolated by immunoprecipitation and identified by LC–ESI-MS/MS. A total of 68 candidate SUMOylated proteins were identified, of which 59 proteins were functionally categorized to gene ontology (GO) terms. Analysis of kyoto encyclopedia of genes and genomes (KEGG) pathways showed that 46 of the identified proteins were involved in 76 pathways that mainly play a role in metabolism, spliceosome and ribosome functions, and in RNA transport. Furthermore, SUMOylation of four candidates (polyubiquitin-C-like isoform X1, 3-hydroxyacyl-CoA dehydrogenase, cyclin-related protein FAM58A-like and GTP-binding nuclear protein Ran) were verified by co-immunoprecipitation in Drosophila schneide 2 cells. In addition, 74% of the identified proteins were predicted to have at least one SUMOylation site. The data presented here shed light on the crucial process of protein sumoylation in Bombyx mori. MDPI 2014-12-01 /pmc/articles/PMC4284691/ /pubmed/25470021 http://dx.doi.org/10.3390/ijms151222011 Text en © 2014 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Tang, Xudong
Fu, Xuliang
Hao, Bifang
Zhu, Feng
Xiao, Shengyan
Xu, Li
Shen, Zhongyuan
Identification of Sumoylated Proteins in the Silkworm Bombyx mori
title Identification of Sumoylated Proteins in the Silkworm Bombyx mori
title_full Identification of Sumoylated Proteins in the Silkworm Bombyx mori
title_fullStr Identification of Sumoylated Proteins in the Silkworm Bombyx mori
title_full_unstemmed Identification of Sumoylated Proteins in the Silkworm Bombyx mori
title_short Identification of Sumoylated Proteins in the Silkworm Bombyx mori
title_sort identification of sumoylated proteins in the silkworm bombyx mori
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4284691/
https://www.ncbi.nlm.nih.gov/pubmed/25470021
http://dx.doi.org/10.3390/ijms151222011
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