ARL11, also known as ADP-Ribosylation Factor-Like Tumor Suppressor Protein 1, plays a significant role in cellular functions. It is particularly noted for its potential role in apoptosis, a process of programmed cell death that is crucial for maintaining cellular homeostasis . The protein is encoded by the ARL11 gene, which has been associated with several familial cancers due to its tumor suppressor properties .
The recombinant form of ARL11 is typically produced using bacterial expression systems. The gene encoding ARL11 is cloned into an expression vector, which is then introduced into a bacterial host such as Escherichia coli. The bacteria are cultured under conditions that induce the expression of the recombinant protein. After sufficient growth, the bacterial cells are lysed, and the recombinant ARL11 protein is purified using techniques such as affinity chromatography.
ARL11, like other GTP-binding proteins, undergoes a cycle between inactive GDP-bound and active GTP-bound states. This cycle is crucial for its function in regulating vesicular trafficking and actin remodeling. The protein’s activity is regulated by guanine nucleotide exchange factors (GEFs) that facilitate the exchange of GDP for GTP, and GTPase-activating proteins (GAPs) that enhance the hydrolysis of GTP to GDP .
In its active GTP-bound state, ARL11 interacts with various effector proteins to propagate cellular signals. Structural studies have shown that the conformational changes in ARL11 during the GDP/GTP cycle are essential for its interaction with these effectors .