A curated tissue-specific proteome, phosphoproteome, and kinome map of Drosophila melanogaster with an integrated outlook in circadian physiology

IF 3.9 4区 生物学 Q1 GENETICS & HEREDITY
Sandip Das, Arpita Kannihalli, Srishti Banerjee, Nikita Chakraborty, Sandipan Ray
{"title":"A curated tissue-specific proteome, phosphoproteome, and kinome map of Drosophila melanogaster with an integrated outlook in circadian physiology","authors":"Sandip Das,&nbsp;Arpita Kannihalli,&nbsp;Srishti Banerjee,&nbsp;Nikita Chakraborty,&nbsp;Sandipan Ray","doi":"10.1007/s10142-025-01554-9","DOIUrl":null,"url":null,"abstract":"<div><p>The fruit fly <i>Drosophila melanogaster</i> is a simple multicellular model system widely used in biomedical research. Here, we aimed to curate a comprehensive tissue and organ-specific proteome, phosphoproteome, and kinome atlas of <i>D. melanogaster.</i> Using information from published literature and databases, we have systematically curated the protein expression profiles, phosphorylation patterns, and the associated kinases and phosphatases in 11 tissue types across the different developmental stages and mature <i>D. melanogaster</i> and its derived cell lines. Gene annotation and pathway enrichment analysis were performed using the DAVID. Protein-protein interaction analysis was carried out using STRING, BioGrid, OmniPath, and InWeb-IM. <i>Drosophila</i> kinase and phosphatase gene orthologs in humans and mice were identified through the FlyBase database, utilizing the DRSC integrative ortholog prediction tool. We mapped a total of 18,377 proteins, 9021 phosphoproteins, 433 kinases, and 141 phosphatases in <i>D. melanogaster</i>. Subsequent categorization of the proteins into different tissue types indicated the enrichment of some tissue-specific pathways and expression clusters. We identified 295 and 289 <i>Drosophila</i> kinase orthologs in humans and mice through an ortholog screening. In the rhythmicity analysis, we observed 24-hour periodicity in 5289 transcripts, 678 proteins, 437 phosphoproteins, 166 kinases, and 89 phosphatases. The findings of our study are integrated as a convenient resource for understanding the proteome-level organizations in <i>Drosophila</i>, their oscillating expression, and their tissue-specific roles in maintaining cellular and physiological functions. We anticipate that this study will help to enhance the systems-level analysis of <i>D. melanogaster</i> as a model organism.</p></div>","PeriodicalId":574,"journal":{"name":"Functional & Integrative Genomics","volume":"25 1","pages":""},"PeriodicalIF":3.9000,"publicationDate":"2025-02-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Functional & Integrative Genomics","FirstCategoryId":"99","ListUrlMain":"https://link.springer.com/article/10.1007/s10142-025-01554-9","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"GENETICS & HEREDITY","Score":null,"Total":0}
引用次数: 0

Abstract

The fruit fly Drosophila melanogaster is a simple multicellular model system widely used in biomedical research. Here, we aimed to curate a comprehensive tissue and organ-specific proteome, phosphoproteome, and kinome atlas of D. melanogaster. Using information from published literature and databases, we have systematically curated the protein expression profiles, phosphorylation patterns, and the associated kinases and phosphatases in 11 tissue types across the different developmental stages and mature D. melanogaster and its derived cell lines. Gene annotation and pathway enrichment analysis were performed using the DAVID. Protein-protein interaction analysis was carried out using STRING, BioGrid, OmniPath, and InWeb-IM. Drosophila kinase and phosphatase gene orthologs in humans and mice were identified through the FlyBase database, utilizing the DRSC integrative ortholog prediction tool. We mapped a total of 18,377 proteins, 9021 phosphoproteins, 433 kinases, and 141 phosphatases in D. melanogaster. Subsequent categorization of the proteins into different tissue types indicated the enrichment of some tissue-specific pathways and expression clusters. We identified 295 and 289 Drosophila kinase orthologs in humans and mice through an ortholog screening. In the rhythmicity analysis, we observed 24-hour periodicity in 5289 transcripts, 678 proteins, 437 phosphoproteins, 166 kinases, and 89 phosphatases. The findings of our study are integrated as a convenient resource for understanding the proteome-level organizations in Drosophila, their oscillating expression, and their tissue-specific roles in maintaining cellular and physiological functions. We anticipate that this study will help to enhance the systems-level analysis of D. melanogaster as a model organism.

黑胃果蝇组织特异性蛋白质组、磷酸化蛋白质组和激酶组图谱,在昼夜生理方面具有综合前景
果蝇(Drosophila melanogaster)是一种简单的多细胞模型系统,广泛用于生物医学研究。在这里,我们的目的是建立一个全面的组织和器官特异性蛋白质组,磷蛋白质组和激酶组图谱。利用已发表的文献和数据库的信息,我们系统地整理了不同发育阶段和成熟黑腹龙及其衍生细胞系的11种组织类型的蛋白质表达谱、磷酸化模式以及相关的激酶和磷酸酶。使用DAVID进行基因注释和途径富集分析。蛋白-蛋白互作分析采用STRING、BioGrid、OmniPath和InWeb-IM进行。利用DRSC整合同源预测工具,通过FlyBase数据库鉴定人类和小鼠的果蝇激酶和磷酸酶基因同源物。我们在黑腹龙中共定位了18,377个蛋白,9021个磷酸化蛋白,433个激酶和141个磷酸酶。随后将这些蛋白分类为不同的组织类型,表明一些组织特异性途径和表达簇的富集。通过同源物筛选,我们在人和小鼠中鉴定出295和289个果蝇激酶同源物。在节律性分析中,我们观察到5289个转录本、678个蛋白质、437个磷酸化蛋白、166个激酶和89个磷酸酶具有24小时的周期性。我们的研究结果被整合为了解果蝇蛋白质组水平组织、它们的振荡表达以及它们在维持细胞和生理功能中的组织特异性作用的便利资源。我们期望这项研究将有助于加强作为模式生物的黑腹龙的系统水平分析。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
CiteScore
3.50
自引率
3.40%
发文量
92
审稿时长
2 months
期刊介绍: Functional & Integrative Genomics is devoted to large-scale studies of genomes and their functions, including systems analyses of biological processes. The journal will provide the research community an integrated platform where researchers can share, review and discuss their findings on important biological questions that will ultimately enable us to answer the fundamental question: How do genomes work?
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信