CLIC1 is unique among chloride channels because it can exist both as a soluble cytoplasmic protein and as an integral membrane protein. This dual existence allows CLIC1 to participate in a variety of cellular functions. Structurally, CLIC1 is related to the glutathione S-transferase (GST) superfamily and contains an approximately 240 amino acid sequence at the C-terminus .
The protein can form ion channels in cellular membranes, facilitating the rapid passage of chloride ions across these membranes. This function is essential for maintaining the proper electrical charge and ion balance within cells .
CLIC1 is involved in several critical cellular processes:
Recombinant CLIC1 refers to the protein produced through recombinant DNA technology. This involves inserting the CLIC1 gene into a suitable expression system, such as bacteria or yeast, to produce the protein in large quantities. Recombinant CLIC1 is used in various research applications to study its structure, function, and role in different cellular processes.
The study of CLIC1 has significant clinical implications. For instance, targeting CLIC1 activity has been explored as a potential therapeutic strategy for treating glioblastoma, a type of brain cancer. Inhibitors of CLIC1 have shown promise in reducing the proliferation and invasiveness of glioblastoma stem cells .