| Title: | Molecular structure of a protein-tyrosine/threonine kinase activating p42 mitogen-activated protein (MAP) kinase: MAP kinase kinase |
| Author(s): | Wu J; Harrison JK; Vincent LA; Haystead C; Haystead TA; Michel H; Hunt DF; Lynch KR; Sturgill TW; |
| Address: | "Department of Internal Medicine, University of Virginia, Charlottesville 22908" |
| ISSN/ISBN: | 0027-8424 (Print) 1091-6490 (Electronic) 0027-8424 (Linking) |
| Abstract: | "MAP kinases p42mapk and p44mapk participate in a protein kinase cascade(s) important for signaling in many cell types and contexts. Both MAP kinases are activated in vitro by MAP kinase kinase, a protein-tyrosine and threonine kinase. A MAP kinase kinase cDNA was isolated from a rat kidney library by using peptide sequence data we obtained from MAP kinase kinase isolated from rabbit skeletal muscle. The deduced sequence, containing 393 amino acids (predicted mass, 43.5 kDa), is most similar to byr1 (Bypass of ras1), a yeast protein kinase functioning in the mating pathway induced by pheromones in Schizosaccharomyces pombe. An unusually large insert is present in MAP kinase kinase between domains IX and X and may contribute to protein-protein interactions with MAP kinase. Major (2.7 kilobases) and minor (1.7 kilobases) transcripts are widely expressed in rat tissues and appear to be derived from a single gene" |
| Keywords: | "Amino Acid Sequence Animals Base Sequence Blotting, Northern Blotting, Southern Brain/enzymology Calcium-Calmodulin-Dependent Protein Kinases Cloning, Molecular DNA/biosynthesis/genetics/isolation & purification Female Gene Library Kidney/*enzymology Male;" |
| Notes: | "MedlineWu, J Harrison, J K Vincent, L A Haystead, C Haystead, T A Michel, H Hunt, D F Lynch, K R Sturgill, T W eng DK41077/DK/NIDDK NIH HHS/ GM37537/GM/NIGMS NIH HHS/ HL08223/HL/NHLBI NIH HHS/ Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. 1993/01/01 Proc Natl Acad Sci U S A. 1993 Jan 1; 90(1):173-7. doi: 10.1073/pnas.90.1.173" |
