Premium
Phosphorylation of human eukaryotic elongation factor 1Bγ is regulated by paclitaxel
Author(s) -
Prado Miguel A.,
Casado Pedro,
ZuazuaVillar Pedro,
del Valle Eva,
Artime Noelia,
CabalHierro Lucía,
MartínezCampa Carlos M.,
Lazo Pedro S.,
Ramos Sofía
Publication year - 2007
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200700226
Subject(s) - elongation factor , phosphorylation , hela , paclitaxel , eukaryotic translation elongation factor 1 alpha 1 , phosphatase , microbiology and biotechnology , elongation , microtubule , biology , cell , chemistry , biochemistry , gene , cancer , rna , genetics , ribosome , materials science , ultimate tensile strength , metallurgy
Paclitaxel (Ptx) is an antitumoural drug that inhibits microtubule dynamics, causes G2/M arrest and induces cell death. 2‐D PAGE and MALDI‐TOF‐MS analysis of HeLa cells extracts revealed that Ptx up‐regulates a form of the eukaryotic elongation factor 1Bγ (eEF1Bγ) and down‐regulates another one. This event, linked to the lack of Ptx effect over eEF1Bγ mRNA or protein levels suggested a PTM of this elongation factor. Further 2‐D PAGE analysis followed by a phosphospecific staining with PRO‐Q Diamond showed the staining of the Ptx up‐regulated form only. Moreover, this Ptx up‐regulated form of eEF1Bγ disappears upon treatment with protein phosphatase. Thus, we demonstrate that human eEF1Bγ phosphorylation is regulated by Ptx.