Journal
JOURNAL OF NEUROCHEMISTRY
Volume 121, Issue 3, Pages 343-348Publisher
WILEY-BLACKWELL
DOI: 10.1111/j.1471-4159.2012.07650.x
Keywords
Alzheimer's disease; amyotrophic lateral sclerosis; apoptosis-associated tyrosine kinase; axonal transport; kinesin-1; lemur tyrosine kinase-1
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Funding
- MRC
- Wellcome Trust
- MNDA
- BBSRC
- MRC [G0501573] Funding Source: UKRI
- Medical Research Council [G0501573] Funding Source: researchfish
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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.
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