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Biochemical Feature of LMO2 Interactome and LMO2 Function Prospect

BACKGROUND: LMO2 belongs to the LIM-Only group of LIM domain protein superfamily. It is ubiquitously expressed in different types of tissues and locates either in the nucleus or in the cytoplasm depending on the tissue type. Till now the unique function of LMO2 was considered to be serving as a brid...

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Detalles Bibliográficos
Autores principales: Wang, Wenhao, Chen, Yaxin, Chang, Ying, Sun, Wei
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Scientific Literature, Inc. 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7409384/
https://www.ncbi.nlm.nih.gov/pubmed/32713935
http://dx.doi.org/10.12659/MSMBR.924421
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author Wang, Wenhao
Chen, Yaxin
Chang, Ying
Sun, Wei
author_facet Wang, Wenhao
Chen, Yaxin
Chang, Ying
Sun, Wei
author_sort Wang, Wenhao
collection PubMed
description BACKGROUND: LMO2 belongs to the LIM-Only group of LIM domain protein superfamily. It is ubiquitously expressed in different types of tissues and locates either in the nucleus or in the cytoplasm depending on the tissue type. Till now the unique function of LMO2 was considered to be serving as a bridging or blocking molecule that mediates extensive protein-protein interactions. However, the exactly biological features of LMO2 interactome as well as LMO2 function spectrum remain largely unclear. MATERIAL/METHODS: In this study, yeast 2-hybrid assay was firstly performed using LMO2 as the bait and the characteristic of LMO2 protein interactome was analyzed according to the yeast 2-hybrid data and other relative biological information primarily using bioinformatic method. RESULTS: Our data indicated that LMO2 favored interacting with peptides containing β-sheet structure and having relatively unstable confirmation. Moreover, several LMO2 favored interacting domains were identified, including WD40 repeat, coiled-coil, Ankyrin repeat, Zinc finger, PDZ, and SH3, and functions of these domain-containing members were dramatically enriched in some types of cancers. CONCLUSIONS: Our results revealed a LMO2 favored protein-interaction pattern in both secondary structure and domain level, and concentrated LMO2 function in kinds of cytoplasmic metabolism pathways as well as multiple types of cancers.
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spelling pubmed-74093842020-08-17 Biochemical Feature of LMO2 Interactome and LMO2 Function Prospect Wang, Wenhao Chen, Yaxin Chang, Ying Sun, Wei Med Sci Monit Basic Res Laboratory Research BACKGROUND: LMO2 belongs to the LIM-Only group of LIM domain protein superfamily. It is ubiquitously expressed in different types of tissues and locates either in the nucleus or in the cytoplasm depending on the tissue type. Till now the unique function of LMO2 was considered to be serving as a bridging or blocking molecule that mediates extensive protein-protein interactions. However, the exactly biological features of LMO2 interactome as well as LMO2 function spectrum remain largely unclear. MATERIAL/METHODS: In this study, yeast 2-hybrid assay was firstly performed using LMO2 as the bait and the characteristic of LMO2 protein interactome was analyzed according to the yeast 2-hybrid data and other relative biological information primarily using bioinformatic method. RESULTS: Our data indicated that LMO2 favored interacting with peptides containing β-sheet structure and having relatively unstable confirmation. Moreover, several LMO2 favored interacting domains were identified, including WD40 repeat, coiled-coil, Ankyrin repeat, Zinc finger, PDZ, and SH3, and functions of these domain-containing members were dramatically enriched in some types of cancers. CONCLUSIONS: Our results revealed a LMO2 favored protein-interaction pattern in both secondary structure and domain level, and concentrated LMO2 function in kinds of cytoplasmic metabolism pathways as well as multiple types of cancers. International Scientific Literature, Inc. 2020-07-27 /pmc/articles/PMC7409384/ /pubmed/32713935 http://dx.doi.org/10.12659/MSMBR.924421 Text en © Med Sci Monit, 2020 This work is licensed under Creative Common Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0 (https://creativecommons.org/licenses/by-nc-nd/4.0/) )
spellingShingle Laboratory Research
Wang, Wenhao
Chen, Yaxin
Chang, Ying
Sun, Wei
Biochemical Feature of LMO2 Interactome and LMO2 Function Prospect
title Biochemical Feature of LMO2 Interactome and LMO2 Function Prospect
title_full Biochemical Feature of LMO2 Interactome and LMO2 Function Prospect
title_fullStr Biochemical Feature of LMO2 Interactome and LMO2 Function Prospect
title_full_unstemmed Biochemical Feature of LMO2 Interactome and LMO2 Function Prospect
title_short Biochemical Feature of LMO2 Interactome and LMO2 Function Prospect
title_sort biochemical feature of lmo2 interactome and lmo2 function prospect
topic Laboratory Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7409384/
https://www.ncbi.nlm.nih.gov/pubmed/32713935
http://dx.doi.org/10.12659/MSMBR.924421
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