The deubiquitinase USP38 affects cellular functions through interacting with LSD1

Abstract Background: Deubiquitination is a posttranslational protein modification prevalent in mammalian cells. Deubiquitinases regulate the functions of the target protein by removing its ubiquitin chain. In this study, the effects of the deubiquitinase USP38's functions on the LSD1 protein a...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Liu,Wenbin, Zhang,Qi, Fang,Yuanyuan, Wang,Yanan
Lenguaje:English
Publicado: Sociedad de Biología de Chile 2018
Materias:
Acceso en línea:http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602018000100243
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:scielo:S0716-97602018000100243
record_format dspace
spelling oai:scielo:S0716-976020180001002432019-06-24The deubiquitinase USP38 affects cellular functions through interacting with LSD1Liu,WenbinZhang,QiFang,YuanyuanWang,Yanan LSD1 Deubiquitinase USP38 Proliferation Abstract Background: Deubiquitination is a posttranslational protein modification prevalent in mammalian cells. Deubiquitinases regulate the functions of the target protein by removing its ubiquitin chain. In this study, the effects of the deubiquitinase USP38's functions on the LSD1 protein and on cell physiology were investigated. Materials and methods: Western blotting, real-time quantitative PCR, immunoprecipitation, denaturing immunoprecipitation and luciferase reporter assays were used to analyze the protein stability, protein interactions and changes in the ubiquitin chain. Cell proliferation assays, colony formation assays, drug treatments and western blotting were used to explore the functions of USP38 in cells. Results: The deubiquitinase USP38 stabilizes protein LSD1 in cells by binding LSD1 and cleaving its ubiquitin chain to prevent the degradation of LSD1 by the intracellular proteasome. USP38 enhances the ability of LSD1 to activate signaling pathways and hence promotes cellular abilities of proliferation and colony formation through interacting with LSD1. Furthermore, USP38 enhances the drug tolerance of human colon cancer cells. Conclusions: USP38 is an LSD1-specific deubiquitinase that affects cellular physiology through interacting with LSD1.info:eu-repo/semantics/openAccessSociedad de Biología de ChileBiological Research v.51 20182018-01-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602018000100243en10.1186/s40659-018-0201-8
institution Scielo Chile
collection Scielo Chile
language English
topic LSD1
Deubiquitinase
USP38
Proliferation
spellingShingle LSD1
Deubiquitinase
USP38
Proliferation
Liu,Wenbin
Zhang,Qi
Fang,Yuanyuan
Wang,Yanan
The deubiquitinase USP38 affects cellular functions through interacting with LSD1
description Abstract Background: Deubiquitination is a posttranslational protein modification prevalent in mammalian cells. Deubiquitinases regulate the functions of the target protein by removing its ubiquitin chain. In this study, the effects of the deubiquitinase USP38's functions on the LSD1 protein and on cell physiology were investigated. Materials and methods: Western blotting, real-time quantitative PCR, immunoprecipitation, denaturing immunoprecipitation and luciferase reporter assays were used to analyze the protein stability, protein interactions and changes in the ubiquitin chain. Cell proliferation assays, colony formation assays, drug treatments and western blotting were used to explore the functions of USP38 in cells. Results: The deubiquitinase USP38 stabilizes protein LSD1 in cells by binding LSD1 and cleaving its ubiquitin chain to prevent the degradation of LSD1 by the intracellular proteasome. USP38 enhances the ability of LSD1 to activate signaling pathways and hence promotes cellular abilities of proliferation and colony formation through interacting with LSD1. Furthermore, USP38 enhances the drug tolerance of human colon cancer cells. Conclusions: USP38 is an LSD1-specific deubiquitinase that affects cellular physiology through interacting with LSD1.
author Liu,Wenbin
Zhang,Qi
Fang,Yuanyuan
Wang,Yanan
author_facet Liu,Wenbin
Zhang,Qi
Fang,Yuanyuan
Wang,Yanan
author_sort Liu,Wenbin
title The deubiquitinase USP38 affects cellular functions through interacting with LSD1
title_short The deubiquitinase USP38 affects cellular functions through interacting with LSD1
title_full The deubiquitinase USP38 affects cellular functions through interacting with LSD1
title_fullStr The deubiquitinase USP38 affects cellular functions through interacting with LSD1
title_full_unstemmed The deubiquitinase USP38 affects cellular functions through interacting with LSD1
title_sort deubiquitinase usp38 affects cellular functions through interacting with lsd1
publisher Sociedad de Biología de Chile
publishDate 2018
url http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602018000100243
work_keys_str_mv AT liuwenbin thedeubiquitinaseusp38affectscellularfunctionsthroughinteractingwithlsd1
AT zhangqi thedeubiquitinaseusp38affectscellularfunctionsthroughinteractingwithlsd1
AT fangyuanyuan thedeubiquitinaseusp38affectscellularfunctionsthroughinteractingwithlsd1
AT wangyanan thedeubiquitinaseusp38affectscellularfunctionsthroughinteractingwithlsd1
AT liuwenbin deubiquitinaseusp38affectscellularfunctionsthroughinteractingwithlsd1
AT zhangqi deubiquitinaseusp38affectscellularfunctionsthroughinteractingwithlsd1
AT fangyuanyuan deubiquitinaseusp38affectscellularfunctionsthroughinteractingwithlsd1
AT wangyanan deubiquitinaseusp38affectscellularfunctionsthroughinteractingwithlsd1
_version_ 1718441578962354176