Open AccessMouse Erk-1 gene product is a serine/threonine protein kinase that has the potential to phosphorylate tyrosine.
Author(s) -
Craig M. Crews,
Alessandro Alessandrini,
Raymond L. Erikson
Publication year - 1991
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.88.19.8845
Subject(s) - autophosphorylation , akt3 , c raf , map2k7 , dusp6 , mitogen activated protein kinase kinase , protein tyrosine phosphatase , biochemistry , biology , phosphorylation , protein kinase a , microbiology and biotechnology , mapk/erk pathway , kinase , threonine , phosphatase , serine , cyclin dependent kinase 2 , protein phosphatase 2
Bacterial expression of mouse gene Erk-1 yielded an active kinase with the same substrate specificity shown for ERK1 protein purified from rat cells. Although rat gene ERK1 is believed to encode a serine/threonine kinase based on sequence data and known ERK1 substrate phosphorylation sites, bacterially-produced mouse Erk-1 (bt-Erk-1) autophosphorylated on tyrosine in addition to serine and threonine residues. The bt-Erk-1 protein also had the capacity to reactivate the ribosomal protein S6 kinase (S6KII). Furthermore, treatment of bt-Erk-1 with either serine/threonine-specific phosphatase 2A or tyrosine-specific phosphatase 1B significantly decreased its kinase activity. These findings predict that autophosphorylation may play an important role in Erk-1/ERK1 regulation.