Glyceraldehyde-3-phosphate dehydrogenase interacts with phosphorylated Akt resulting from increased blood glucose in rat cardiac muscle

AbstractHere we describe the interaction of phosphorylated ∼40kDa protein with phosphorylated Akt which is a serine/threonine kinase resulting from increased blood glucose in rat cardiac muscle. Mass spectrometry analysis revealed that this protein was glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Furthermore, increase in Akt and GAPDH phosporylation and induction of their association were both observed after insulin stimulation in the H9c2 cell line derived from embryonic rat ventricle. Moreover, the activation of GAPDH was upregulated when the GAPDH phosphorylation was increased. Our data suggest that GAPDH phosphorylation and association with Akt by insulin treatment have some bearing on the enhancement of GAPDH activity.Structured summaryMINT-7891324, MINT-7891304, MINT-7891314: GAPDH (uniprotkb:P04797) physically interacts (MI:0915) with Akt (uniprotkb:P47196) by anti bait coimmunoprecipitation (MI:0006

Crystallization and preliminary X-ray diffraction studies of the ISC-like [2Fe–2S] ferredoxin (FdxB) from Pseudomonas putida JCM 20004

A vertebrate-type [2Fe–2S] ferredoxin (FdxB), which is probably involved in the iron–sulfur cluster-biosynthesis system of the γ-proteobacterium P. putida JCM 20004, has been crystallized in space group P6122. The needle-shaped crystals of recombinant FdxB diffract to 1.90 Å resolution using synchrotron radiation