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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Thornton, Claire Bright, Nicola J. Carling, David |
| Description | Author Affiliation: Bright NJ ( Medical Research Council Cellular Stress Group, MRC Clinical Sciences Centre, Du Cane Road, London, United Kingdom.) |
| Abstract | Brain-specific kinases 1 and 2 (BRSK1/2) are AMP-activated protein kinase (AMPK)-related kinases that are highly expressed in mammalian forebrain. Studies using transgenic animal models have implicated a role for these kinases in the establishment of neuronal polarity. BRSK1 and BRSK2 are activated by phosphorylation of a threonine residue in the T-loop activation segment of the kinase domain. In vitro studies have demonstrated that LKB1, an upstream kinase in the AMPK cascade, can catalyze this phosphorylation. However, to date, a detailed comparative analysis of the molecular regulation of BRSK1/2 has not been undertaken. Here we present evidence that excludes another upstream kinase in the AMPK cascade, Ca(2+)/calmodulin-dependent protein kinase kinase beta, from a role in activating BRSK1/2. We show that equivalent mutations in the ubiquitin-associated domains of the BRSK isoforms produce differential effects on the activation of BRSK1 and BRSK2. Contrary to previous reports, activation of cAMP-dependent protein kinase does not affect BRSK1 or BRSK2 activity in mammalian cells. Furthermore, stimuli that activate AMPK had no effect on BRSK1/2. Finally, we provide evidence suggesting that protein phosphatase 2C is a likely candidate for catalyzing the dephosphorylation and inactivation of BRSK1/2. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 22 |
| Volume Number | 283 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2008-05-30 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Intracellular Signaling Peptides And Proteins Metabolism Phosphoprotein Phosphatases Protein-Serine-Threonine Kinases Animals Calcium-Calmodulin-Dependent Protein Kinase Type 1 Cell Line Enzyme Activation Physiology Gene Expression Regulation, Enzymologic Genetics Isoenzymes Mutation Phosphorylation Prosencephalon Enzymology Protein Kinases Protein Structure, Tertiary Rabbits Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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