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Phosphorylation of nm23-H1 by CKI induces its complex formation with h-prune and promotes cell motility

Title data

Garzia, Livia ; D'Angelo, A. ; Amoresano, A. ; Knauer, Shirley K. ; Cirulli, C. ; Campanella, C. ; Stauber, R. H. ; Steegborn, Clemens ; Iolascon, A. ; Zollo, Massimo:
Phosphorylation of nm23-H1 by CKI induces its complex formation with h-prune and promotes cell motility.
In: Oncogene. Vol. 27 (20 March 2008) Issue 13 . - pp. 1853-1864.
ISSN 1476-5594
DOI: https://doi.org/10.1038/sj.onc.1210822

Abstract in another language

The combination of an increase in the cAMP-phosphodiesterase activity of h-prune and its interaction with nm23-H1 have been shown to be key steps in the induction of cellular motility in breast cancer cells. Here we present the molecular mechanisms of this interaction. The region of the nm23-h-prune interaction lies between S120 and S125 of nm23, where missense mutants show impaired binding; this region has been highly conserved throughout evolution, and can undergo serine phosphorylation by casein kinase I. Thus, the casein kinase I delta-epsilon specific inhibitor IC261 impairs the formation of the nm23-h-prune complex, which translates 'in vitro' into inhibition of cellular motility in a breast cancer cellular model. A competitive permeable peptide containing the region for phosphorylation by casein kinase I impairs cellular motility to the same extent as IC261. The identification of these two modes of inhibition of formation of the nm23-H1-h-prune protein complex pave the way toward new challenges, including translational studies using IC261 or this competitive peptide 'in vivo' to inhibit cellular motility induced by nm23-H1-h-prune complex formation during progression of breast cancer.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 17906697
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry > Chair Biochemistry - Univ.-Prof. Dr. Clemens Steegborn
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry
Result of work at the UBT: No
DDC Subjects: 500 Science > 540 Chemistry
Date Deposited: 14 Apr 2015 10:44
Last Modified: 12 Apr 2016 11:47
URI: https://eref.uni-bayreuth.de/id/eprint/10144