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Analysis of PTEN ubiquitylation and SUMOylation using molecular traps
- Source :
- Methods. :112-118
- Publication Year :
- 2015
- Publisher :
- Elsevier BV, 2015.
-
Abstract
- The function of the tumour suppressor phosphatase and tensin homolog deleted on chromosome 10 (PTEN) is tightly controlled by post-translational modifications (PTMs) including ubiquitin or Small Ubiquitin-related MOdifiers (SUMO). It is known that SUMOylation by SUMO-1, SUMO-2/-3, mono- or polyubiquitylation have a distinct impact on PTEN activity, localisation and/or stability, however the molecular mechanisms governing these processes are still unclear. Studying PTM regulated events has always been a difficult task due to their labile nature. Here, we propose an update on the role of these PTMs on PTEN function, as well as a methodological overview on the use of molecular traps named SUMO Binding Entities (SUBEs) or Tandem Ubiquitin Binding Entities (TUBEs) to capture SUMOylated or Ubiquitylated forms of PTEN respectively. When combined with in vitro SUMOylation or Ubiquitylation assays, the use of molecular traps facilitate the detection of modified forms of PTEN. SUMO and ubiquitin-traps are also suitable to capture endogenously modified forms of PTEN after expression of E3 ligases or treatment with chemical inhibitors. This versatile approach represents an interesting alternative to explore PTEN regulation by SUMO and ubiquitin under physiological or pathological conditions.
- Subjects :
- biology
Ubiquitin binding
Tumor Suppressor Proteins
PTEN Phosphohydrolase
Ubiquitination
SUMO protein
Sumoylation
SUMO binding
General Biochemistry, Genetics and Molecular Biology
Cell biology
HEK293 Cells
Proteasome
Ubiquitin
biology.protein
Cancer research
Humans
Tensin
PTEN
Protein Processing, Post-Translational
Molecular Biology
Function (biology)
Subjects
Details
- ISSN :
- 10462023
- Database :
- OpenAIRE
- Journal :
- Methods
- Accession number :
- edsair.doi.dedup.....869e17c6cbaef3a4dc63d836be0c0e9c
- Full Text :
- https://doi.org/10.1016/j.ymeth.2014.09.001