E3 ligase UHRF2 stabilizes the acetyltransferase TIP60 and regulates H3K9ac and H3K14ac via RING finger domain
Protein & Cell
;
(12): 202-218, 2017.
Artículo
en Inglés
| WPRIM
| ID: wpr-757377
ABSTRACT
UHRF2 is a ubiquitin-protein ligase E3 that regulates cell cycle, genomic stability and epigenetics. We conducted a co-immunoprecipitation assay and found that TIP60 and HDAC1 interact with UHRF2. We previously demonstrated that UHRF2 regulated H3K9ac and H3K14ac differentially in normal and cancer cells. However, the accurate signal transduction mechanisms were not clear. In this study, we found that TIP60 acted downstream of UHRF2 to regulate H3K9ac and H3K14ac expression. TIP60 is stabilized in normal cells by UHRF2 ubiquitination. However, TIP60 is destabilized in cancer cells. Depletion or inhibition of TIP60 disrupts the regulatory relationship between UHRF2, H3K9ac and H3K14ac. In summary, the findings suggest that UHRF2 mediated the post-translational modification of histones and the initiation and progression of cancer.
Texto completo:
Disponible
Índice:
WPRIM (Pacífico Occidental)
Asunto principal:
Histonas
/
Línea Celular
/
Ubiquitina-Proteína Ligasas
/
Histona Acetiltransferasas
/
Dominios RING Finger
/
Ubiquitinación
/
Lisina Acetiltransferasa 5
/
Genética
/
Metabolismo
/
Proteínas de Neoplasias
Límite:
Humanos
Idioma:
Inglés
Revista:
Protein & Cell
Año:
2017
Tipo del documento:
Artículo
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