PIP4K II Alpha and Beta
This is a recent project to create 3D printed models of PIP4K II Alpha and Beta. These models were commissioned by Cornell University for the purpose of demonstrating PIP4K dimerization.
Phosphatidylinositol 4-kinases are evolutionarily conserved among eukaryotes and include four human isoforms.
- phosphatidylinositol 4-kinase alpha (PI4KA)
- phosphatidylinositol 4-kinase beta (PI4KB)
- phosphatidylinositol 4-kinase 2-alpha (PI4K2A)
- phosphatidylinositol 4-kinase 2-beta (PI4K2B)
Phosphatidylinositol 4-kinase (PI4K) is an essential molecule in the cellular signaling and trafficking especially in the Golgi apparatus and the trans-Golgi network. This family of protein is an intracellular protein that traffics between the cytoplasm and nucleus. In the cytoplasm, Pi4KKB can be recruited to the membranes of the Golgi apparatus by GTP binding proteins Arf1 and Rab11. PI4KB is phosphorylated by kinase D. This interaction with stabilizes PI4K in an active conformation and regulates the trafficking from the Golgi system to the plasma membrane. Its nuclear function remains is not yet fully understood, and the study of its structure remains of significance.
Phosphatidylinositol 4-kinase 2-alpha (PI4K2A) is the most abundant phosphatidylinositol 4-kinase in human cells and is responsible for the synthesis of approximately 50% of the total PI4P within the cell. PI4K2A is associated mainly with the membranes of the trans-Golgi network and early and late endosomes; its membrane association is achieved by a heavy palmitoylation within a specific cysteine-rich motif. Besides the synthesis of phosphatidylinositol 4,5-bisphosphate, PI4K2A is involved in various cellular processes including membrane trafficking, regulation of endosomal sorting promoting target protein recruitment to endosomes or trans-Golgi network, or signal transduction. Particularly, it regulates e.g. targeting of clathrin adaptor complexes to the Golgi apparatus, the Wnt signaling, or EGFR signaling pathway.
Phosphatidylinositol 4-kinase 2-beta (PI4K2B) is primarily cytosolic and contributes to overall PI4-kinase activity along with other protein family members. This protein is involved in early T cell activation and insulin signaling.
PIP4K kinases are composed of a proline-rich N-terminal region, a central helical domain, and a kinase domain located C-terminally. The N-terminal region contains a physiologically important binding site for a Golgi adaptor protein ACBD3. The central helical domain is responsible for the interaction with a small guanosine triphosphatase Rab11. Like most kinases, PIP4K can be divided into N-terminal and C-terminal lobes with the ATP binding groove and putative phosphatidylinositol binding pocket in a cleft between the lobes.
PIP4K kinases can be found in vivo as both monomers and dimers.
Purchase 3D Prints of PIP4K II Alpha and Beta
Models available in mutltiple sizes and printed to order. Purchase two of each and demonstrate protein dimerization. Please allow for two weeks for printing and shipping.
Contact or Questions
Please feel free to email us if you have any questions, comments or requests.