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Identifying novel SMYD3 interactors on the trail of cancer hallmarks

SMYD3 overexpression in several human cancers highlights its crucial role in carcinogenesis. Nonetheless, SMYD3 specific activity in cancer development and progression is currently under debate. Taking advantage of a library of rare tripeptides, which we first tested for their in vitro binding affin...

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Detalles Bibliográficos
Autores principales: Fasano, Candida, Lepore Signorile, Martina, De Marco, Katia, Forte, Giovanna, Sanese, Paola, Grossi, Valentina, Simone, Cristiano
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Research Network of Computational and Structural Biotechnology 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9039736/
https://www.ncbi.nlm.nih.gov/pubmed/35495117
http://dx.doi.org/10.1016/j.csbj.2022.03.037
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author Fasano, Candida
Lepore Signorile, Martina
De Marco, Katia
Forte, Giovanna
Sanese, Paola
Grossi, Valentina
Simone, Cristiano
author_facet Fasano, Candida
Lepore Signorile, Martina
De Marco, Katia
Forte, Giovanna
Sanese, Paola
Grossi, Valentina
Simone, Cristiano
author_sort Fasano, Candida
collection PubMed
description SMYD3 overexpression in several human cancers highlights its crucial role in carcinogenesis. Nonetheless, SMYD3 specific activity in cancer development and progression is currently under debate. Taking advantage of a library of rare tripeptides, which we first tested for their in vitro binding affinity to SMYD3 and then used as in silico probes, we recently identified BRCA2, ATM, and CHK2 as direct SMYD3 interactors. To gain insight into novel SMYD3 cancer-related roles, here we performed a comprehensive in silico analysis to cluster all potential SMYD3-interacting proteins identified by screening the human proteome for the previously tested tripeptides, based on their involvement in cancer hallmarks. Remarkably, we identified mTOR, BLM, MET, AMPK, and p130 as new SMYD3 interactors implicated in cancer processes. Further studies are needed to characterize the functional mechanisms underlying these interactions. Still, these findings could be useful to devise novel therapeutic strategies based on the combined inhibition of SMYD3 and its newly identified molecular partners. Of note, our in silico methodology may be useful to search for unidentified interactors of other proteins of interest.
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spelling pubmed-90397362022-04-28 Identifying novel SMYD3 interactors on the trail of cancer hallmarks Fasano, Candida Lepore Signorile, Martina De Marco, Katia Forte, Giovanna Sanese, Paola Grossi, Valentina Simone, Cristiano Comput Struct Biotechnol J Research Article SMYD3 overexpression in several human cancers highlights its crucial role in carcinogenesis. Nonetheless, SMYD3 specific activity in cancer development and progression is currently under debate. Taking advantage of a library of rare tripeptides, which we first tested for their in vitro binding affinity to SMYD3 and then used as in silico probes, we recently identified BRCA2, ATM, and CHK2 as direct SMYD3 interactors. To gain insight into novel SMYD3 cancer-related roles, here we performed a comprehensive in silico analysis to cluster all potential SMYD3-interacting proteins identified by screening the human proteome for the previously tested tripeptides, based on their involvement in cancer hallmarks. Remarkably, we identified mTOR, BLM, MET, AMPK, and p130 as new SMYD3 interactors implicated in cancer processes. Further studies are needed to characterize the functional mechanisms underlying these interactions. Still, these findings could be useful to devise novel therapeutic strategies based on the combined inhibition of SMYD3 and its newly identified molecular partners. Of note, our in silico methodology may be useful to search for unidentified interactors of other proteins of interest. Research Network of Computational and Structural Biotechnology 2022-04-11 /pmc/articles/PMC9039736/ /pubmed/35495117 http://dx.doi.org/10.1016/j.csbj.2022.03.037 Text en © 2022 The Authors. Published by Elsevier B.V. on behalf of Research Network of Computational and Structural Biotechnology. https://creativecommons.org/licenses/by/4.0/This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Research Article
Fasano, Candida
Lepore Signorile, Martina
De Marco, Katia
Forte, Giovanna
Sanese, Paola
Grossi, Valentina
Simone, Cristiano
Identifying novel SMYD3 interactors on the trail of cancer hallmarks
title Identifying novel SMYD3 interactors on the trail of cancer hallmarks
title_full Identifying novel SMYD3 interactors on the trail of cancer hallmarks
title_fullStr Identifying novel SMYD3 interactors on the trail of cancer hallmarks
title_full_unstemmed Identifying novel SMYD3 interactors on the trail of cancer hallmarks
title_short Identifying novel SMYD3 interactors on the trail of cancer hallmarks
title_sort identifying novel smyd3 interactors on the trail of cancer hallmarks
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9039736/
https://www.ncbi.nlm.nih.gov/pubmed/35495117
http://dx.doi.org/10.1016/j.csbj.2022.03.037
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