L3MBTL3 is induced by HIF-1&#945; and fine tunes the HIF-1&#945; degradation under hypoxia in vitro.

Wang, Mengdong; Wang, Di; Lang, Yue; Shao, Anwen; Zhang, Rui; Tang, Jun; Lai, Dongming; Xiao, Chenglu

L3MBTL3 is induced by HIF-1α and fine tunes the HIF-1α degradation under hypoxia in vitro.

Wang, Mengdong; Wang, Di; Lang, Yue; Shao, Anwen; Zhang, Rui; Tang, Jun; Lai, Dongming; Xiao, Chenglu.

Afiliación

Wang M; National Key Laboratory of Veterinary Public Health Security, College of Veterinary Medicine, China Agricultural University, Beijing, 100193, China.
Wang D; National Key Laboratory of Veterinary Public Health Security, College of Veterinary Medicine, China Agricultural University, Beijing, 100193, China.
Lang Y; National Key Laboratory of Veterinary Public Health Security, College of Veterinary Medicine, China Agricultural University, Beijing, 100193, China.
Shao A; National Key Laboratory of Veterinary Public Health Security, College of Veterinary Medicine, China Agricultural University, Beijing, 100193, China.
Zhang R; National Key Laboratory of Veterinary Public Health Security, College of Veterinary Medicine, China Agricultural University, Beijing, 100193, China.
Tang J; National Key Laboratory of Veterinary Public Health Security, College of Veterinary Medicine, China Agricultural University, Beijing, 100193, China.
Lai D; Sun Yat-sen Memorial Hospital, Sun Yat-sen University, NO. 107, Yanjiangxi Road, Guangzhou, 510120, China.
Xiao C; National Key Laboratory of Veterinary Public Health Security, College of Veterinary Medicine, China Agricultural University, Beijing, 100193, China.

Heliyon ; 9(2): e13222, 2023 Feb.

Article en En | MEDLINE | ID: mdl-36747531

ABSTRACT

ABSTRACT

HIF-1α plays a crucial part in hypoxia response by transcriptionally upregulating genes to adapt the hypoxic condition. HIF-1α is under severe cellular control as its exceptional activation is always associated with tumorigenesis and tumor progression. Here, we report L3MBTL3 serves as a novel negative regulator of HIF-1α. It is upregulated during hypoxia and acts as a transcriptional target of HIF-1α. In the nuclei, L3MBTL3 makes an interaction with HIF-1α and promotes its ubiquitination and degradation. These findings indicate L3MBTL3 forms a negative feedback loop with HIF-1α in vitro to dampen the hypoxic response.

Palabras clave

ARNT, aryl hydrocarbon receptor nuclear translocator; CHX, cycloheximide; FCS, phenylalanine-cysteine-serine nucleic acid−binding; HIF-1, hypoxia inducible factor 1; HIF-1α; HIF-1α degradation; HRE, hypoxia response element; Hypoxia; L3MBTL3; L3MBTL3, lethal (3) malignant brain tumor-like 3; MBT, malignant brain tumor; PHD, prolyl hydroxylase domain; SAM, sterile α motif; VHL, von Hippel-Lindau

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