MARK1 is a member of the MARK family and is a serine/threonine-protein kinase that plays a key role in signal transduction. Due to its protein serine/threonine kinase activity, MARK1 is known to mediate phosphorylation of key proteins involved in signal transduction and cell communication. MARK1 phosphorylates microtubule-associated proteins and trigger microtubule disruption. Gene mutation studies performed in mice revealed that after targeted disruption of the MARK1 gene, the mice lacked the ability to drink, and displayed hind leg motor dysfunction.
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MARK phosphorylates the microtubule-associated proteins tau, MAP2, and MAP4 on their microtubule-binding domain, causing their dissociation from microtubules and increased microtubule dynamics. We describe the molecular cloning, distribution, activation mechanism, and overexpression of two MARK proteins from rat that arise
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 20(10), 1718-1720 (2006-06-30)
Given that thousands of genes exist in the mammalian genome, criteria are needed to prioritize their functional analysis and to decrease the likelihood of producing gene-targeted mice that lack overt phenotypes. Initial analysis efforts are likely to be fruitful if
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