Rattray, M. (2012) New insights on regulation of LMTK2, a membrane kinase integrating pathways central to neurodegeneration. Journal of Neurochemistry, 121 (3). pp. 327-328. ISSN 0022-3042 doi: 10.1111/j.1471-4159.2012.07654.x
Abstract/Summary
In a short communication in this issue (Manser et al. 2012), Christopher Miller’s group at the Institute of Psychiatry, King’s College London present an elegant and convincing set of experiments using molecular techniques to show that a brain-enriched membrane-associated protein kinase, lemur tyrosine kinase-2 (LMTK2), is directly phosphorylated by the cyclin-dependent kinase-5/p35 and this event is sufficient for LMTK2 to phosphorylate an abundant protein phosphatase, PP1C. LMTK2 has been little studied to date and, despite its name, is a kinase which phosphorylates serine or threonine residues of protein substrates. The paper adds to the evidence that this enzyme is a potentially important mediator positioned to integrate a number of intracellular signalling pathways relevant to neurodegeneration.
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| Item Type | Article |
| URI | https://reading-clone.eprints-hosting.org/id/eprint/26261 |
| Identification Number/DOI | 10.1111/j.1471-4159.2012.07654.x |
| Refereed | Yes |
| Divisions | Life Sciences > School of Chemistry, Food and Pharmacy > School of Pharmacy > Division of Pharmacology Interdisciplinary Research Centres (IDRCs) > Centre for Integrative Neuroscience and Neurodynamics (CINN) |
| Publisher | Wiley-Blackwell |
| Download/View statistics | View download statistics for this item |
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