Cdk5/p35 phosphorylates lemur tyrosine kinase-2 to regulate protein phosphatase-1C phosphorylation and activity

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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 languageEnglish
Article numberN/A
Pages (from-to)343-348
Number of pages6
JournalJournal of Neurochemistry
Volume121
Issue number3
DOIs
Publication statusPublished - 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

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