Panneerselvam S, Marx A, Mandelkow EM, Mandelkow E.
Structure of the catalytic and ubiquitin-associated domains of the protein kinase MARK/Par-1.
Structure. 2006 Feb;14(2):173-83.
PubMed.
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.
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University of Pennsylvania
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.
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