Abstract
Cyclin-dependent kinase-5 (cdk5)/p35 and protein phosphatase-1 (PP1) are two major enzymes that control a variety of physiological processes within the nervous system including neuronal differentiation, synaptic plasticity and axonal transport. Defective cdk5/p35 and PP1 function are also implicated in several major human neurodegenerative diseases. Cdk5/p35 and the catalytic subunit of PP1 (PP1C) both bind to the brain-enriched, serinethreonine kinase lemur tyrosine kinase-2 (LMTK2). Moreover, LMTK2 phosphorylates PP1C on threonine-320 (PP1Cthr320) to inhibit its activity. Here, we demonstrate that LMTK2 is phosphorylated on serine-1418 (LMTK2ser1418) by cdk5/p35 and present evidence that this regulates its ability to phosphorylate PP1Cthr320. We thus describe a new signalling pathway within the nervous system that links cdk5/p35 with PP1C and which has implications for a number of neuronal functions and neuronal dysfunction.
Original language | English |
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Article number | N/A |
Pages (from-to) | 343-348 |
Number of pages | 6 |
Journal | Journal of Neurochemistry |
Volume | 121 |
Issue number | 3 |
DOIs | |
Publication status | Published - May 2012 |
Keywords
- Alzheimer's disease
- amyotrophic lateral sclerosis
- apoptosis-associated tyrosine kinase
- axonal transport
- kinesin-1
- lemur tyrosine kinase-1
- CYCLIN-DEPENDENT KINASE-5
- AXONAL-TRANSPORT
- MYOSIN-VI
- BRAIN
- NEUROFILAMENTS
- BREK/LMTK2
- NEURONS