PMID- 25224693
OWN - NLM
STAT- MEDLINE
DCOM- 20160115
LR  - 20161125
IS  - 1095-9130 (Electronic)
IS  - 1046-2023 (Linking)
VI  - 77-78
DP  - 2015 May
TI  - Analysis of PTEN ubiquitylation and SUMOylation using molecular traps.
PG  - 112-8
LID - S1046-2023(14)00287-4 [pii]
LID - 10.1016/j.ymeth.2014.09.001 [doi]
AB  - 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.
CI  - Copyright (c) 2014 Elsevier Inc. All rights reserved.
FAU - Lang, Valerie
AU  - Lang V
AD  - Inbiomed, Ubiquitylation and Cancer Molecular Biology Laboratory, Cancer Unit 
      Mikeletegi 81, 20009 San Sebastian-Donostia, Spain. Electronic address: 
      vlang@inbiomed.org.
FAU - Aillet, Fabienne
AU  - Aillet F
AD  - Inbiomed, Ubiquitylation and Cancer Molecular Biology Laboratory, Cancer Unit 
      Mikeletegi 81, 20009 San Sebastian-Donostia, Spain. Electronic address: 
      faillet@inbiomed.org.
FAU - Da Silva-Ferrada, Elisa
AU  - Da Silva-Ferrada E
AD  - Inbiomed, Ubiquitylation and Cancer Molecular Biology Laboratory, Cancer Unit 
      Mikeletegi 81, 20009 San Sebastian-Donostia, Spain. Electronic address: 
      edasilva@inbiomed.org.
FAU - Xolalpa, Wendy
AU  - Xolalpa W
AD  - Inbiomed, Ubiquitylation and Cancer Molecular Biology Laboratory, Cancer Unit 
      Mikeletegi 81, 20009 San Sebastian-Donostia, Spain. Electronic address: 
      wendyxolalpa@gmail.com.
FAU - Zabaleta, Lorea
AU  - Zabaleta L
AD  - Inbiomed, Ubiquitylation and Cancer Molecular Biology Laboratory, Cancer Unit 
      Mikeletegi 81, 20009 San Sebastian-Donostia, Spain. Electronic address: 
      lzabaleta@inbiomed.org.
FAU - Rivas, Carmen
AU  - Rivas C
AD  - Dpt Biologia Molecular y Celular, Centro Nacional de Biotecnologia-CSIC, Darwin 
      3, Madrid 28049, Spain; Centro de Investigacion en Medicina Molecular y 
      Enfermedades Cronicas (CIMUS), Universidad de Santiago de Compostela, Instituto 
      de Investigaciones Sanitarias (IDIS), Santiago de Compostela E15706, Spain. 
      Electronic address: mcarmen.rivas@usc.es.
FAU - Rodriguez, Manuel S
AU  - Rodriguez MS
AD  - Inbiomed, Ubiquitylation and Cancer Molecular Biology Laboratory, Cancer Unit 
      Mikeletegi 81, 20009 San Sebastian-Donostia, Spain. Electronic address: 
      msrodriguez@inbiomed.org.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20140916
PL  - United States
TA  - Methods
JT  - Methods (San Diego, Calif.)
JID - 9426302
RN  - 0 (Tumor Suppressor Proteins)
RN  - EC 3.1.3.67 (PTEN Phosphohydrolase)
RN  - EC 3.1.3.67 (PTEN protein, human)
SB  - IM
MH  - HEK293 Cells
MH  - Humans
MH  - PTEN Phosphohydrolase/*genetics/*metabolism
MH  - Protein Processing, Post-Translational/physiology
MH  - Sumoylation/*physiology
MH  - Tumor Suppressor Proteins/*genetics/*metabolism
MH  - Ubiquitination/*physiology
OTO - NOTNLM
OT  - Degradation
OT  - PTEN
OT  - Proteasome
OT  - Proteolysis
OT  - SUMOylation
OT  - Ubiquitylation
EDAT- 2014/09/17 06:00
MHDA- 2016/01/16 06:00
CRDT- 2014/09/17 06:00
PHST- 2014/07/21 00:00 [received]
PHST- 2014/08/29 00:00 [revised]
PHST- 2014/09/03 00:00 [accepted]
PHST- 2014/09/17 06:00 [entrez]
PHST- 2014/09/17 06:00 [pubmed]
PHST- 2016/01/16 06:00 [medline]
AID - S1046-2023(14)00287-4 [pii]
AID - 10.1016/j.ymeth.2014.09.001 [doi]
PST - ppublish
SO  - Methods. 2015 May;77-78:112-8. doi: 10.1016/j.ymeth.2014.09.001. Epub 2014 Sep 
      16.