Gankyrin consists of seven ankyrin repeats, which are structural motifs involved in protein-protein interactions . These repeats allow Gankyrin to interact with various cellular proteins, including the S6 ATPase of the 19S regulatory particle of the 26S proteasome . This interaction is essential for the degradation of ubiquitinated proteins, a process critical for maintaining cellular homeostasis.
Gankyrin is known to enhance the phosphorylation of the retinoblastoma protein (Rb) by CDK4, leading to the progression of the cell cycle . Additionally, it promotes the ubiquitination and subsequent degradation of the tumor suppressor protein p53 by MDM2 . These actions contribute to the oncogenic properties of Gankyrin, facilitating uncontrolled cell proliferation and survival in cancer cells.
Recombinant human Gankyrin is produced using Escherichia coli (E. coli) expression systems . The recombinant protein typically corresponds to the amino acids 1-226 of the human Gankyrin sequence and is purified using conventional chromatography techniques . It is often used in research to study the protein’s structure, function, and interactions, as well as its role in cancer progression.
Recombinant Gankyrin is utilized in various biochemical and cellular assays to investigate its interactions with other proteins and its effects on cellular processes . It is also used in drug discovery efforts aimed at identifying inhibitors that can block Gankyrin’s oncogenic activities, offering potential therapeutic strategies for treating cancers associated with its overexpression.