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Protein Prenyltransferases and Their Inhibitors: Structural and Functional Characterization
Protein prenylation is a post-translational modification controlling the localization, activity, and protein–protein interactions of small GTPases, including the Ras superfamily. This covalent attachment of either a farnesyl (15 carbon) or a geranylgeranyl (20 carbon) isoprenoid group is catalyzed b...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9141697/ https://www.ncbi.nlm.nih.gov/pubmed/35628237 http://dx.doi.org/10.3390/ijms23105424 |
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author | Marchwicka, Aleksandra Kamińska, Daria Monirialamdari, Mohsen Błażewska, Katarzyna M. Gendaszewska-Darmach, Edyta |
author_facet | Marchwicka, Aleksandra Kamińska, Daria Monirialamdari, Mohsen Błażewska, Katarzyna M. Gendaszewska-Darmach, Edyta |
author_sort | Marchwicka, Aleksandra |
collection | PubMed |
description | Protein prenylation is a post-translational modification controlling the localization, activity, and protein–protein interactions of small GTPases, including the Ras superfamily. This covalent attachment of either a farnesyl (15 carbon) or a geranylgeranyl (20 carbon) isoprenoid group is catalyzed by four prenyltransferases, namely farnesyltransferase (FTase), geranylgeranyltransferase type I (GGTase-I), Rab geranylgeranyltransferase (GGTase-II), and recently discovered geranylgeranyltransferase type III (GGTase-III). Blocking small GTPase activity, namely inhibiting prenyltransferases, has been proposed as a potential disease treatment method. Inhibitors of prenyltransferase have resulted in substantial therapeutic benefits in various diseases, such as cancer, neurological disorders, and viral and parasitic infections. In this review, we overview the structure of FTase, GGTase-I, GGTase-II, and GGTase-III and summarize the current status of research on their inhibitors. |
format | Online Article Text |
id | pubmed-9141697 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-91416972022-05-28 Protein Prenyltransferases and Their Inhibitors: Structural and Functional Characterization Marchwicka, Aleksandra Kamińska, Daria Monirialamdari, Mohsen Błażewska, Katarzyna M. Gendaszewska-Darmach, Edyta Int J Mol Sci Review Protein prenylation is a post-translational modification controlling the localization, activity, and protein–protein interactions of small GTPases, including the Ras superfamily. This covalent attachment of either a farnesyl (15 carbon) or a geranylgeranyl (20 carbon) isoprenoid group is catalyzed by four prenyltransferases, namely farnesyltransferase (FTase), geranylgeranyltransferase type I (GGTase-I), Rab geranylgeranyltransferase (GGTase-II), and recently discovered geranylgeranyltransferase type III (GGTase-III). Blocking small GTPase activity, namely inhibiting prenyltransferases, has been proposed as a potential disease treatment method. Inhibitors of prenyltransferase have resulted in substantial therapeutic benefits in various diseases, such as cancer, neurological disorders, and viral and parasitic infections. In this review, we overview the structure of FTase, GGTase-I, GGTase-II, and GGTase-III and summarize the current status of research on their inhibitors. MDPI 2022-05-12 /pmc/articles/PMC9141697/ /pubmed/35628237 http://dx.doi.org/10.3390/ijms23105424 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Marchwicka, Aleksandra Kamińska, Daria Monirialamdari, Mohsen Błażewska, Katarzyna M. Gendaszewska-Darmach, Edyta Protein Prenyltransferases and Their Inhibitors: Structural and Functional Characterization |
title | Protein Prenyltransferases and Their Inhibitors: Structural and Functional Characterization |
title_full | Protein Prenyltransferases and Their Inhibitors: Structural and Functional Characterization |
title_fullStr | Protein Prenyltransferases and Their Inhibitors: Structural and Functional Characterization |
title_full_unstemmed | Protein Prenyltransferases and Their Inhibitors: Structural and Functional Characterization |
title_short | Protein Prenyltransferases and Their Inhibitors: Structural and Functional Characterization |
title_sort | protein prenyltransferases and their inhibitors: structural and functional characterization |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9141697/ https://www.ncbi.nlm.nih.gov/pubmed/35628237 http://dx.doi.org/10.3390/ijms23105424 |
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