MARK/PAR1 kinase is a regulator of microtubule-dependent transport in axons. - AlzForum Alzheimer Research Paper of the Week


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Home: Papers of the Week

Annotation

	Mandelkow EM, Thies E, Trinczek B, Biernat J, Mandelkow E. MARK/PAR1 kinase is a regulator of microtubule-dependent transport in axons. J Cell Biol. 2004 Oct 11;167(1):99-110. PubMed Abstract

	Comments on Related Papers

	Related Paper: Structure of the catalytic and ubiquitin-associated domains of the protein kinase MARK/Par-1. Comment by: Virginia Lee, ARF Advisor
	Submitted 15 February 2006 \| Permalink	Posted 15 February 2006
	The Mandelkows have managed to decipher the x-ray crystallographic structure of the part of MARK2 that is involved in the regulation of the binding of tau to microtubules through phosphorylation at specific sites. This is clearly a major and important accomplishment. Furthermore, they were also able to identify a novel property of MARK2 by demonstrating the presence of a ubiquitin-associated domain in MARK2. The importance of obtaining the crystal structure of MARK2 is that it should enable the design of better inhibitors that may reduce phosphorylation of tau and increase its binding to microtubules. This could stabilize microtubules in the degenerating axons of Alzheimer disease. View all comments by Virginia Lee

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REAGENTS/MATERIAL:

Antibodies and dyes used in these experiments were rat monoclonal anti-tubulin antibody YL1/2 and mouse mAb DM1A purchased from Serotec and Sigma-Aldrich, respectively (1:2,000); and polyclonal rabbit HA tag antibody (MoBiTec). Polyclonal rabbit anti tau-antibody K9JA (DakoCytomation), mAb 12E8 against tau (gift from P. Seubert, Elan Pharma), and antibodies against peroxisomes (gift ofW. Just, University of Heidelberg). The clone of mRFP was provided by R. Tsien (University of California, San Diego). All fluorescent (TRITC, FITC, and AMCA) secondary antibodies were purchased from Dianova.