Open AccessMolecular cloning and expression of a 90-kDa diacylglycerol kinase that predominantly localizes in neurons.
Author(s) -
Kaoru Goto,
Hisatake Kondo
Publication year - 1993
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.90.16.7598
Subject(s) - diacylglycerol kinase , complementary dna , biology , microbiology and biotechnology , protein kinase c , biochemistry , protein kinase a , map2k7 , cdna library , cyclin dependent kinase 9 , mitogen activated protein kinase kinase , kinase , cyclin dependent kinase 2 , gene
A diacylglycerol kinase cDNA was isolated from a rat brain cDNA library. This cDNA encoded an 801-amino acid protein of 90,287 Da. This 90-kDa diacylglycerol kinase showed 58% identity in deduced amino acid sequence with a previously isolated rat 80-kDa diacylglycerol kinase. EF-hand motifs, cysteine-rich zinc-finger-like sequences, and putative ATP-binding sites were all conserved between the two kinase species. However, mRNA encoding the 90-kDa kinase was confined to restricted neuronal populations such as the caudate-putamen, the accumbens nucleus, and the olfactory tubercle. Further, the 90-kDa kinase was found to exhibit high phosphorylation activity for long-chain diacylglycerols and was mainly associated with the membrane fraction when the cDNA was transfected into COS-7 cells.