Literature DB >> 27761832

Assessing the Role of Paralog-Specific Sumoylation of HDAC1.

Simona Citro1, Susanna Chiocca2.   

Abstract

Attachment of ubiquitin or ubiquitin-like (Ubl) modifiers, such as the small ubiquitin-related modifier SUMO, is a posttranslational modification (PTM) that reversibly regulates the function and the stability of target proteins. The SUMO paralogs SUMO1 and SUMO2/3, although sharing a common conjugation pathway, seem to play different roles in the cell. Many regulatory mechanisms, which contribute to SUMO-paralog-specific modification, have emerged. We have recently found that cell environment affects SUMO-paralog-specific sumoylation of HDAC1, whose conjugation to SUMO1 and not to SUMO2 facilitates its protein turnover. Here, we describe how to identify SUMO-paralog-specific conjugation of HDAC1 and how the different expression of SUMO E3 ligases in the cell plays an important role in this mechanism.

Entities:  

Keywords:  HDAC; HDAC1; PIASy; PTM; SUMO1; SUMO2/3

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Substances:

Year:  2017        PMID: 27761832     DOI: 10.1007/978-1-4939-6527-4_24

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN: 1064-3745


  1 in total

1.  Histone deacetylase 1 induced by neddylation inhibition contributes to drug resistance in acute myelogenous leukemia.

Authors:  Qiu-Yu Lai; Ying-Zhi He; Xiong-Wen Peng; Xuan Zhou; Dan Liang; Liang Wang
Journal:  Cell Commun Signal       Date:  2019-07-29       Impact factor: 5.712

  1 in total

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