Direct and indirect roles of GRWD1 in the inactivation of p53 in cancer | Zendy

Mai Koizumi Ichikawa | Zendy; Masao Saitoh | Zendy

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Direct and indirect roles of GRWD1 in the inactivation of p53 in cancer

Author(s) -

Mai Koizumi Ichikawa,

Masao Saitoh

Publication year - 2022

Publication title -

the journal of biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.28

H-Index - 115

eISSN - 1756-2651

pISSN - 0021-924X

DOI - 10.1093/jb/mvac010

Subject(s) - ubiquitin ligase , mdm2 , ubiquitin , transcription (linguistics) , chemistry , microbiology and biotechnology , cell cycle , p53 protein , cell , biology , biochemistry , apoptosis , gene , linguistics , philosophy

Glutamate-rich WD40 repeat containing 1 (GRWD1), also known as WDR28, interacts with various proteins through its WD domain and is involved in transcription, translation, cell cycle progression, ubiquitin-mediated degradation and DNA replication and repair. Ribosomal protein L11 (RPL11), which directly interacts with MDM2, inhibits MDM2 ubiquitin ligase activity, thus promoting p53 stabilization. Binding of GRWD1 to RPL11 disrupts the interaction between RPL11 and MDM2 and promotes p53 ubiquitination by MDM2. In addition, a recent report by Fujiyama et al. found that GRWD1 also directly interacts with wild-type p53 and suppresses its transcriptional activity. They propose that GRWD1 is a novel tumor-promoting molecule that negatively regulates wild-type p53 via both indirect and direct mechanisms.

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