title: Analysis of PTEN ubiquitylation and SUMOylation using molecular traps.
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.
authors.affiliation: Inbiomed, Ubiquitylation and Cancer Molecular Biology Laboratory, Cancer Unit Mikeletegi 81, 20009 San Sebastián-Donostia, Spain. Electronic address: vlang@inbiomed.org.
authors.forename: Valérie
authors.initials: V
authors.lastname: Lang
authors.affiliation: Inbiomed, Ubiquitylation and Cancer Molecular Biology Laboratory, Cancer Unit Mikeletegi 81, 20009 San Sebastián-Donostia, Spain. Electronic address: faillet@inbiomed.org.
authors.forename: Fabienne
authors.initials: F
authors.lastname: Aillet
authors.affiliation: Inbiomed, Ubiquitylation and Cancer Molecular Biology Laboratory, Cancer Unit Mikeletegi 81, 20009 San Sebastián-Donostia, Spain. Electronic address: edasilva@inbiomed.org.
authors.forename: Elisa
authors.initials: E
authors.lastname: Da Silva-Ferrada
authors.affiliation: Inbiomed, Ubiquitylation and Cancer Molecular Biology Laboratory, Cancer Unit Mikeletegi 81, 20009 San Sebastián-Donostia, Spain. Electronic address: wendyxolalpa@gmail.com.
authors.forename: Wendy
authors.initials: W
authors.lastname: Xolalpa
authors.affiliation: Inbiomed, Ubiquitylation and Cancer Molecular Biology Laboratory, Cancer Unit Mikeletegi 81, 20009 San Sebastián-Donostia, Spain. Electronic address: lzabaleta@inbiomed.org.
authors.forename: Lorea
authors.initials: L
authors.lastname: Zabaleta
authors.affiliation: Dpt Biología Molecular y Celular, Centro Nacional de Biotecnología-CSIC, Darwin 3, Madrid 28049, Spain; Centro de Investigación en Medicina Molecular y Enfermedades Crónicas (CIMUS), Universidad de Santiago de Compostela, Instituto de Investigaciones Sanitarias (IDIS), Santiago de Compostela E15706, Spain. Electronic address: mcarmen.rivas@usc.es.
authors.forename: Carmen
authors.initials: C
authors.lastname: Rivas
authors.affiliation: Inbiomed, Ubiquitylation and Cancer Molecular Biology Laboratory, Cancer Unit Mikeletegi 81, 20009 San Sebastián-Donostia, Spain. Electronic address: msrodriguez@inbiomed.org.
authors.forename: Manuel S
authors.initials: MS
authors.lastname: Rodriguez
mesh_terms: D057809:HEK293 Cells; D006801:Humans; D051059:PTEN Phosphohydrolase / Q000235:genetics* / Q000378:metabolism*; D011499:Protein Processing, Post-Translational / Q000502:physiology; D058207:Sumoylation / Q000502:physiology*; D025521:Tumor Suppressor Proteins / Q000235:genetics* / Q000378:metabolism*; D054875:Ubiquitination / Q000502:physiology*
chemical_list: D025521:Tumor Suppressor Proteins; D051059:PTEN Phosphohydrolase; C494929:PTEN protein, human
keywords: Degradation; PTEN; Proteasome; Proteolysis; SUMOylation; Ubiquitylation