P57^Kip2 Phosphorylation Modulates Its Localization, Stability, and Interactions.

ABSTRACT: p57^Kip2 is a member of the cyclin-dependent kinase (CDK) Interacting Protein/Kinase Inhibitory Protein (CIP/Kip) family that also includes p21^Cip1/WAF1 and p27^Kip1. Different from its siblings, few data are available about the p57^Kip2 protein, especially in humans. Structurally, p57^Kip2 is an intrinsically unstructured protein, a characteristic that confers functional flexibility with multiple transient interactions influencing the metabolism and roles of the protein. Being an IUP, its localization, stability, and binding to functional partners might be strongly modulated by post-translational modifications, especially phosphorylation. In this work, we investigated by two-dimensional analysis the phosphorylation pattern of p57^Kip2

SUBMITTER: Stampone E 

PROVIDER: S-EPMC11508627 | biostudies-literature | 2024 Oct

REPOSITORIES: biostudies-literature