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Conjugated Protein Domains as Engineered Scaffold Proteins
[Image: see text] Assembly of proteins into higher-order complexes generates specificity and selectivity in cellular signaling. Signaling complex formation is facilitated by scaffold proteins that use modular scaffolding domains, which recruit specific pathway enzymes. Multimerization and recombinat...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical
Society
2020
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7303964/ https://www.ncbi.nlm.nih.gov/pubmed/32374984 http://dx.doi.org/10.1021/acs.bioconjchem.0c00183 |
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author | Lemmens, Lenne J. M. Ottmann, Christian Brunsveld, Luc |
author_facet | Lemmens, Lenne J. M. Ottmann, Christian Brunsveld, Luc |
author_sort | Lemmens, Lenne J. M. |
collection | PubMed |
description | [Image: see text] Assembly of proteins into higher-order complexes generates specificity and selectivity in cellular signaling. Signaling complex formation is facilitated by scaffold proteins that use modular scaffolding domains, which recruit specific pathway enzymes. Multimerization and recombination of these conjugated native domains allows the generation of libraries of engineered multidomain scaffold proteins. Analysis of these engineered proteins has provided molecular insight into the regulatory mechanism of the native scaffold proteins and the applicability of these synthetic variants. This topical review highlights the use of engineered, conjugated multidomain scaffold proteins on different length scales in the context of synthetic signaling pathways, metabolic engineering, liquid–liquid phase separation, and hydrogel formation. |
format | Online Article Text |
id | pubmed-7303964 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | American Chemical
Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-73039642020-06-19 Conjugated Protein Domains as Engineered Scaffold Proteins Lemmens, Lenne J. M. Ottmann, Christian Brunsveld, Luc Bioconjug Chem [Image: see text] Assembly of proteins into higher-order complexes generates specificity and selectivity in cellular signaling. Signaling complex formation is facilitated by scaffold proteins that use modular scaffolding domains, which recruit specific pathway enzymes. Multimerization and recombination of these conjugated native domains allows the generation of libraries of engineered multidomain scaffold proteins. Analysis of these engineered proteins has provided molecular insight into the regulatory mechanism of the native scaffold proteins and the applicability of these synthetic variants. This topical review highlights the use of engineered, conjugated multidomain scaffold proteins on different length scales in the context of synthetic signaling pathways, metabolic engineering, liquid–liquid phase separation, and hydrogel formation. American Chemical Society 2020-05-06 2020-06-17 /pmc/articles/PMC7303964/ /pubmed/32374984 http://dx.doi.org/10.1021/acs.bioconjchem.0c00183 Text en Copyright © 2020 American Chemical Society This is an open access article published under a Creative Commons Non-Commercial No Derivative Works (CC-BY-NC-ND) Attribution License (http://pubs.acs.org/page/policy/authorchoice_ccbyncnd_termsofuse.html) , which permits copying and redistribution of the article, and creation of adaptations, all for non-commercial purposes. |
spellingShingle | Lemmens, Lenne J. M. Ottmann, Christian Brunsveld, Luc Conjugated Protein Domains as Engineered Scaffold Proteins |
title | Conjugated Protein Domains as Engineered Scaffold
Proteins |
title_full | Conjugated Protein Domains as Engineered Scaffold
Proteins |
title_fullStr | Conjugated Protein Domains as Engineered Scaffold
Proteins |
title_full_unstemmed | Conjugated Protein Domains as Engineered Scaffold
Proteins |
title_short | Conjugated Protein Domains as Engineered Scaffold
Proteins |
title_sort | conjugated protein domains as engineered scaffold
proteins |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7303964/ https://www.ncbi.nlm.nih.gov/pubmed/32374984 http://dx.doi.org/10.1021/acs.bioconjchem.0c00183 |
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