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Cell Oncol (Dordr) ; 47(3): 1065-1070, 2024 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-38150153

RESUMO

STAT3 is a pleiotropic transcription factor overactivated in 70% of solid tumours. We have recently reported that inactivating mutations on residues susceptible to post-translational modifications (PTMs) in only one of the monomers (i.e. asymmetric) caused changes in the cellular distribution of STAT3 homodimers. Here, we used more controlled experimental conditions, i.e. without the interference of endogenous STAT3 (STAT3-/- HeLa cells) and in the presence of a defined cytokine stimulus (Leukemia Inhibitory Factor, LIF), to provide further evidence that asymmetric PTMs affect the nuclear translocation of STAT3 homodimers. Time-lapse microscopy for 20 min after LIF stimulation showed that S727 dephosphorylation (S727A) and K685 inactivation (K685R) slightly enhanced the nuclear translocation of STAT3 homodimers, while K49 inactivation (K49R) delayed STAT3 nuclear translocation. Our findings suggest that asymmetrically modified STAT3 homodimers could be a new level of STAT3 regulation and, therefore, a potential target for cancer therapy.


Assuntos
Núcleo Celular , Fator Inibidor de Leucemia , Multimerização Proteica , Processamento de Proteína Pós-Traducional , Fator de Transcrição STAT3 , Humanos , Transporte Ativo do Núcleo Celular , Núcleo Celular/metabolismo , Células HeLa , Fator Inibidor de Leucemia/metabolismo , Fosforilação , Transporte Proteico/efeitos dos fármacos , Fator de Transcrição STAT3/metabolismo
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