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Updated: May 29, 2026

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
Published on: May 3, 2018
Elk-1 interacts with dynein upon serum stimulation but independent of serine 383 phosphorylation
Ozlem Demir1, Oya Ari, Isil Aksan Kurnaz
1Department of Genetics and Bioengineering, Yeditepe University, 26 Agustos Yerlesimi, Kayisdagi, 34755 Istanbul, Turkey. demir@mpi-cbg.de
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.
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