title: Elk-1 interacts with dynein upon serum stimulation but independent of serine 383 phosphorylation.
abstract: Elk-1 belongs to the Ternary Complex Factor (TCF) subfamily of the ETS (from E26 viral oncogene) domain superfamily of transcription factors, and has been known as a regulator of mitogen-induced immediate early gene transcription upon Mitogen Activated Protein Kinase (MAPK) activation. Elk-1 has been previously shown to interact with neuronal microtubules, and here we show that P-S383-Elk-1, in addition to co-localizing with motor proteins kinesin, Eg5 and Mitotik Kinesin-Like Protein (MKLP) at the mitotic spindles, it physically interacts with dynein in a serum induction-dependent but Ser383 phosphorylation-independent manner.
authors.affiliation: Department of Genetics and Bioengineering, Yeditepe University, 26 Agustos Yerlesimi, Kayisdagi, 34755 Istanbul, Turkey. demir@mpi-cbg.de
authors.forename: Ozlem
authors.initials: O
authors.lastname: Demir
authors.forename: Oya
authors.initials: O
authors.lastname: Ari
authors.forename: Isil Aksan
authors.initials: IA
authors.lastname: Kurnaz
mesh_terms: D000818:Animals; D045744:Cell Line, Tumor; D004247:DNA / Q000378:metabolism; D004398:Dyneins / Q000378:metabolism*; D006801:Humans; D010766:Phosphorylation; D010768:Phosphoserine / Q000378:metabolism*; D011485:Protein Binding; D021381:Protein Transport; D051381:Rats; D044967:Serum / Q000378:metabolism*; D014404:Tubulin / Q000378:metabolism; D050807:ets-Domain Protein Elk-1 / Q000378:metabolism*
chemical_list: D014404:Tubulin; D050807:ets-Domain Protein Elk-1; D010768:Phosphoserine; D004247:DNA; D004398:Dyneins