A mouse brain cDNA encodes a novel protein with the protein kinase C phosphorylation site domain common to MARCKS
- 29 July 1991
- journal article
- Published by Wiley in FEBS Letters
- Vol. 286 (1-2) , 147-151
- https://doi.org/10.1016/0014-5793(91)80961-2
Abstract
We have isolated a mouse brain cDNA clone encoding a protein of 200 amino acids (Mr, 20165) with partial homology with MARCKS (myristoylated alanine-rich C-kinase substrate). Two regions show similarity with MARCKS, one is the kinase C phosphorylation site domain which is supposed to bind calmodulin, and the other is the region near to the N-terminus, including the consensus sequence of myristoylation. It has a similar amino acid composition to MARCKS, but the content of alanine is not as high. It is distributed throughout the mouse brain, but the pattern is not identical with that of MARCKS. Both proteins may be members of a new protein family involved in coupling the protein kinase C and calmodulin signal transduction systemsKeywords
This publication has 20 references indexed in Scilit:
- A Collection of cDNA Clones with Specific Expression Patterns in Mouse BrainEuropean Journal of Neuroscience, 1990
- Localization of the MARCKS (87 kDa) protein, a major specific substrate for protein kinase C, in rat brainJournal of Neuroscience, 1990
- SEQUENCES OF INTEREST: Molecular Cloning, Sequence, and Expression of a cDNA Encoding the Chicken Myristoylated Alanine-Rich C Kinase Substrate (MARCKS)Molecular Endocrinology, 1989
- Molecular cloning, characterization, and expression of a cDNA encoding the "80- to 87-kDa" myristoylated alanine-rich C kinase substrate: a major cellular substrate for protein kinase C.Proceedings of the National Academy of Sciences, 1989
- Phosphorylation and associated translocation of the 87-kDa protein, a major protein kinase C substrate, in isolated nerve terminals.Proceedings of the National Academy of Sciences, 1989
- Stimulus-dependent myristoylation of a major substrate for protein kinase CNature, 1988
- The 87-kDa protein, a major specific substrate for protein kinase C: purification from bovine brain and characterization.Proceedings of the National Academy of Sciences, 1987
- Studies and Perspectives of Protein Kinase CScience, 1986
- Phorbol esters, phospholipase C, and growth factors rapidly stimulate the phosphorylation of a Mr 80,000 protein in intact quiescent 3T3 cells.Proceedings of the National Academy of Sciences, 1983
- Calcium/phospholipid regulates phosphorylation of a Mr "87k" substrate protein in brain synaptosomes.Proceedings of the National Academy of Sciences, 1982