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Updated: Jun 5, 2026

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
Published on: May 3, 2018
Structurally constrained residues outside the binding motif are essential in the interaction of 14-3-3 and
Marina Uhart1, Alberto A Iglesias, Diego M Bustos
1Instituto Tecnológico de Chascomús (IIB-INTECH, CONICET-UNSAM), Camino Circunvalación Laguna, Km 6 cc164, Chascomus B7130IWA, Argentina.
Abstract:
14-3-3 proteins participate in many key cellular processes after binding to disordered phospho-partners. Usually, the phosphorylated state is an essential target for the binding. Here, we show for the first time residues other than those in the 14-3-3 binding motif that are essential for the binding between 14-3-3 and a phosphorylated partner. Results support that phosphorylation, although necessary, is not sufficient for 14-3-3's complex formation, as structurally constrained anchor residues play a critical function in stabilizing the protein-protein interaction.
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