New potential peptide therapeutics perturbing CK1δ/α-tubulin interaction

Marc Krüger, Hubert Kalbacher, Panagiotis L. Kastritis, Joachim Bischof, Holger Barth, Doris Henne-Bruns, Constantinos Vorgias, Stefania Sarno, Lorenzo A. Pinna, Uwe Knippschild

Research output: Contribution to journalArticlepeer-review

6 Scopus citations


Members of the CK1 family are highly conserved serine/threonine specific kinases being expressed in all eukaryotes. They are involved in many cellular processes and therefore tightly regulated. A central mechanism to modulate CK1 activity is via interaction with cellular proteins. CK1δ interacts with α-/β-tubulin and is involved in the regulation of microtubule dynamics. Therefore, it is important to identify the structural elements responsible for the interaction between these proteins. Using a peptide library covering the human CK1δ amino acid sequence in SPR and ELISA analyses, we identified peptide 39 (P39), encompassing aa361-aa375 of CK1δ, as a prominent binding partner of α-tubulin. P39 decreases α-tubulin phosphorylation by CK1δ and reduces the thermodynamic stability of α-tubulin in fluorescence thermal shift assays. Furthermore, P39 induces an inhibition of mitotic progression and a disruption of cells entering mitosis in CV-1 cells. Taken together our data provide valuable information regarding the interaction of CK1δ and α-tubulin and a novel approach for the development of pharmacological tools to inhibit proliferation of cancer cells.

Original languageEnglish
Pages (from-to)375-383
Number of pages9
JournalCancer Letters
Issue number2
StatePublished - 1 Jun 2016
Externally publishedYes


  • CK1
  • Microtubules
  • Mitosis
  • Peptide therapeutics


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