Post-translational modifications on the retinoblastoma protein
Abstract The retinoblastoma protein (pRb) functions as a cell cycle regulator controlling G1 to S phase transition and plays critical roles in tumour suppression. It is frequently inactivated in various tumours. The functions of pRb are tightly regulated, where post-translational modifications (PTMs...
Main Authors: | , , , , , , |
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Format: | Article |
Language: | English |
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BMC
2022-06-01
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Series: | Journal of Biomedical Science |
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Online Access: | https://doi.org/10.1186/s12929-022-00818-x |
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author | Linbin Zhou Danny Siu-Chun Ng Jason C. Yam Li Jia Chen Clement C. Tham Chi Pui Pang Wai Kit Chu |
author_facet | Linbin Zhou Danny Siu-Chun Ng Jason C. Yam Li Jia Chen Clement C. Tham Chi Pui Pang Wai Kit Chu |
author_sort | Linbin Zhou |
collection | DOAJ |
description | Abstract The retinoblastoma protein (pRb) functions as a cell cycle regulator controlling G1 to S phase transition and plays critical roles in tumour suppression. It is frequently inactivated in various tumours. The functions of pRb are tightly regulated, where post-translational modifications (PTMs) play crucial roles, including phosphorylation, ubiquitination, SUMOylation, acetylation and methylation. Most PTMs on pRb are reversible and can be detected in non-cancerous cells, playing an important role in cell cycle regulation, cell survival and differentiation. Conversely, altered PTMs on pRb can give rise to anomalies in cell proliferation and tumourigenesis. In this review, we first summarize recent findings pertinent to how individual PTMs impinge on pRb functions. As many of these PTMs on pRb were published as individual articles, we also provide insights on the coordination, either collaborations and/or competitions, of the same or different types of PTMs on pRb. Having a better understanding of how pRb is post-translationally modulated should pave the way for developing novel and specific therapeutic strategies to treat various human diseases. |
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format | Article |
id | doaj.art-65563937304245b09d21717b99aafc59 |
institution | Directory Open Access Journal |
issn | 1423-0127 |
language | English |
last_indexed | 2024-04-12T13:34:34Z |
publishDate | 2022-06-01 |
publisher | BMC |
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series | Journal of Biomedical Science |
spelling | doaj.art-65563937304245b09d21717b99aafc592022-12-22T03:31:02ZengBMCJournal of Biomedical Science1423-01272022-06-0129111610.1186/s12929-022-00818-xPost-translational modifications on the retinoblastoma proteinLinbin Zhou0Danny Siu-Chun Ng1Jason C. Yam2Li Jia Chen3Clement C. Tham4Chi Pui Pang5Wai Kit Chu6Department of Ophthalmology & Visual Sciences, The Chinese University of Hong KongDepartment of Ophthalmology & Visual Sciences, The Chinese University of Hong KongDepartment of Ophthalmology & Visual Sciences, The Chinese University of Hong KongDepartment of Ophthalmology & Visual Sciences, The Chinese University of Hong KongDepartment of Ophthalmology & Visual Sciences, The Chinese University of Hong KongDepartment of Ophthalmology & Visual Sciences, The Chinese University of Hong KongDepartment of Ophthalmology & Visual Sciences, The Chinese University of Hong KongAbstract The retinoblastoma protein (pRb) functions as a cell cycle regulator controlling G1 to S phase transition and plays critical roles in tumour suppression. It is frequently inactivated in various tumours. The functions of pRb are tightly regulated, where post-translational modifications (PTMs) play crucial roles, including phosphorylation, ubiquitination, SUMOylation, acetylation and methylation. Most PTMs on pRb are reversible and can be detected in non-cancerous cells, playing an important role in cell cycle regulation, cell survival and differentiation. Conversely, altered PTMs on pRb can give rise to anomalies in cell proliferation and tumourigenesis. In this review, we first summarize recent findings pertinent to how individual PTMs impinge on pRb functions. As many of these PTMs on pRb were published as individual articles, we also provide insights on the coordination, either collaborations and/or competitions, of the same or different types of PTMs on pRb. Having a better understanding of how pRb is post-translationally modulated should pave the way for developing novel and specific therapeutic strategies to treat various human diseases.https://doi.org/10.1186/s12929-022-00818-xRetinoblastomaPhosphorylationUbiquitinationSUMOylationAcetylationMethylation |
spellingShingle | Linbin Zhou Danny Siu-Chun Ng Jason C. Yam Li Jia Chen Clement C. Tham Chi Pui Pang Wai Kit Chu Post-translational modifications on the retinoblastoma protein Journal of Biomedical Science Retinoblastoma Phosphorylation Ubiquitination SUMOylation Acetylation Methylation |
title | Post-translational modifications on the retinoblastoma protein |
title_full | Post-translational modifications on the retinoblastoma protein |
title_fullStr | Post-translational modifications on the retinoblastoma protein |
title_full_unstemmed | Post-translational modifications on the retinoblastoma protein |
title_short | Post-translational modifications on the retinoblastoma protein |
title_sort | post translational modifications on the retinoblastoma protein |
topic | Retinoblastoma Phosphorylation Ubiquitination SUMOylation Acetylation Methylation |
url | https://doi.org/10.1186/s12929-022-00818-x |
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