title: Functional regulation of TEL by p38-induced phosphorylation.
abstract: TEL is a nuclear phosphoprotein that belongs to a member of the ETS family transcription factors. TEL acts as a tumor suppressor and is essential for establishing hematopoiesis in neonatal bone marrow. Because TEL possesses multiple putative mitogen-activated protein (MAP) kinase phosphorylation sites, we here investigated functional regulation of TEL via stress signaling pathways. We showed that TEL becomes phosphorylated in vivo by activated p38 but not by JNK1. The constitutive and inducible phosphorylation sites were found to be Ser(22) and Ser(257), respectively. TEL bound to p38 and was directly phosphorylated in vitro by p38. In vivo p38-dependent phosphorylation reduced trans-repressional abilities of TEL through ETS-binding consensus site. These data indicate that TEL's functions are potentially regulated by p38 which is activated by various kinds of stresses. TEL could be a constituent downstream of the specific MAP kinase in the signal transduction system.
authors.affiliation: Department of Hematology, Dokkyo University School of Medicine, 321-0293, Tochigi, Japan.
authors.forename: Honoka
authors.initials: H
authors.lastname: Arai
authors.forename: Kazuhiro
authors.initials: K
authors.lastname: Maki
authors.forename: Kazuo
authors.initials: K
authors.lastname: Waga
authors.forename: Ko
authors.initials: K
authors.lastname: Sasaki
authors.forename: Yuichi
authors.initials: Y
authors.lastname: Nakamura
authors.forename: Yoichi
authors.initials: Y
authors.lastname: Imai
authors.forename: Mineo
authors.initials: M
authors.lastname: Kurokawa
authors.forename: Hisamaru
authors.initials: H
authors.lastname: Hirai
authors.forename: Kinuko
authors.initials: K
authors.lastname: Mitani
mesh_terms: D000818:Animals; D015153:Blotting, Western; D019556:COS Cells; D004268:DNA-Binding Proteins / Q000096:biosynthesis* / Q000235:genetics*; D017353:Gene Deletion; D005786:Gene Expression Regulation; D005982:Glutathione Transferase / Q000378:metabolism; D006367:HeLa Cells; D006801:Humans; D008156:Luciferases / Q000378:metabolism; D020928:Mitogen-Activated Protein Kinases / Q000378:metabolism*; D009154:Mutation; D010766:Phosphorylation; D010957:Plasmids / Q000378:metabolism; D011233:Precipitin Tests; D011485:Protein Binding; D050783:Proto-Oncogene Proteins c-ets; D012097:Repressor Proteins / Q000096:biosynthesis* / Q000235:genetics*; D012694:Serine / Q000378:metabolism; D015398:Signal Transduction; D048051:p38 Mitogen-Activated Protein Kinases; D000097764:ETS Translocation Variant 6 Protein
chemical_list: D004268:DNA-Binding Proteins; D005982:Glutathione Transferase; D008156:Luciferases; D020928:Mitogen-Activated Protein Kinases; D050783:Proto-Oncogene Proteins c-ets; D012097:Repressor Proteins; D012694:Serine; D048051:p38 Mitogen-Activated Protein Kinases; D000097764:ETS Translocation Variant 6 Protein