| First Author | Berson AE | Year | 1999 |
| Journal | Biochem Biophys Res Commun | Volume | 259 |
| Issue | 3 | Pages | 533-8 |
| PubMed ID | 10364453 | Mgi Jnum | J:55702 |
| Mgi Id | MGI:1339226 | Doi | 10.1006/bbrc.1999.0811 |
| Citation | Berson AE, et al. (1999) Identification and characterization of a myristylated and palmitylated serine/threonine protein kinase. Biochem Biophys Res Commun 259(3):533-8 |
| abstractText | We report the molecular cloning and initial characterization of a novel fatty acid acylated serine/threonine protein kinase. The putative open reading frame is predicted to encode a 305 amino acid protein possessing a carboxy-terminal protein kinase domain and amino-terminal myristylation and palmitylation sites. The protein kinase has been accordingly denoted as the myristylated and palmitylated serine/threonine protein kinase (MPSK). Human and mouse MPSKs share approximately 93% identity at the amino acid level with complete retention of acylation sites. Radiation hybridization localized the human MPSK gene to chromosome 2q34-37. Northern analysis demonstrated that the human MPSK 1.7 kilobase mRNA is widely distributed. Epitope tagged human MPSK was found to be acylated by myristic acid at glycine residue 2 and by palmitic acid at cysteines 6 and/or 8. Palmitylation of MPSK in these experiments was found to require an intact myristylation site. While epitope tagged MPSK in immune complexes or purified human glutathione S transferase-MPSK was found to autophosphorylate at one or more threonine residues, the enzyme was not found to phosphorylate several other common exogenous substrates. Indeed, only PHAS-I was identified as an exogenous substrate which was found to be phosphorylated on threonine and serine residues. Copyright 1999 Academic Press. |
