Post-translational modifications on the retinoblastoma protein

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 cr...

Full description

Saved in:
Bibliographic Details
Published inJournal of biomedical science Vol. 29; no. 1; pp. 33 - 16
Main Authors Zhou, Linbin, Ng, Danny Siu-Chun, Yam, Jason C, Chen, Li Jia, Tham, Clement C, Pang, Chi Pui, Chu, Wai Kit
Format Journal Article
LanguageEnglish
Published England BioMed Central Ltd 01.06.2022
BioMed Central
BMC
Subjects
Online AccessGet full text

Cover

Loading…
More Information
Summary: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.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
ObjectType-Review-3
content type line 23
ISSN:1423-0127
1021-7770
1423-0127
DOI:10.1186/s12929-022-00818-x