Ca²⁺ -induced structural changes and intramolecular interactions in N-terminal region of diacylglycerol kinase alpha.

ABSTRACT: Diacylglycerol kinases (DGKs) are multi-domain lipid kinases that modulate the levels of lipid messengers, diacylglycerol, and phosphatidic acid. Recently, increasing attention has been paid to its α isozyme (DGKα) as a potential target for cancer immunotherapy. However, little progress has been made on the structural biology of DGKs, and a detailed understanding of the Ca²⁺ -triggered activation of DGKα, for which the N-terminal domains likely play a critical role, remains unclear. We have recently shown that Ca²⁺ binding to DGKα-EF induces conformational changes from a protease-susceptible "open" conformation in the apo state to a well-folded one in its holo state. Here, we further studied the structural properties of DGKα N-terminal (RVH and EF) domains using a ser

SUBMITTER: Takahashi D 

PROVIDER: S-EPMC9202544 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature