The activation loop of phosphatidylinositol phosphate kinases determines signaling specificity.

摘要: Abstract Phosphatidylinositol-4,5-bisphosphate plays a pivotal role in the regulation of cell proliferation and survival, cytoskeletal reorganization, membrane trafficking. However, little is known about temporal spatial its synthesis. Higher eukaryotic cells have potential to use two distinct pathways for generation phosphatidylinositol-4,5-bisphosphate. These require classes phosphatidylinositol phosphate kinases, termed type I II PIP kinases. While highly related by sequence, these kinases localize different subcellular compartments, phosphorylate substrates, are functionally nonredundant. Here, we show that 20– 25–amino acid loop spanning catalytic site, activation loop, determines both enzymatic specificity targeting Therefore, controls signaling kinase function at multiple levels.