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J Biol Chem, Vol. 274, Issue 48, 33847-33850, November 26, 1999
From the Friedrich Miescher-Institut, Maulbeerstrasse
66, CH-4058 Basel, Switzerland
Ndr is a nuclear serine/threonine protein kinase
that belongs to a subfamily of kinases implicated in the regulation of
cell division and cell morphology. This subfamily includes the kinases LATS, Orb6, Cot-1, and Dbf2. We show here that Ndr is potently activated when intact cells are treated with okadaic acid, suggesting that Ndr is normally held in a state of low activity by protein phosphatase 2A. We mapped the regulatory phosphorylation sites of Ndr
protein kinase and found that active Ndr is phosphorylated on Ser-281
and Thr-444. Mutation of either site to alanine strongly reduced both
basal and okadaic acid-stimulated Ndr activity, while combined mutation
abolished Ndr activity completely. Importantly, each of these sites
(and also the surrounding sequences) are conserved in the kinase
relatives of Ndr, suggesting a general mechanism of activation for
kinases of this subfamily. Ser-281 and Thr-444 are also similar to the
regulatory phosphorylation sites in several targets of the
phosphoinositide-dependent protein kinase
PDK1.1 However, PDK1
does not appear to function as an upstream kinase for Ndr. Thus, Ndr
and its close relatives may operate in a novel signaling pathway
downstream of an as-yet-unidentified kinase with specificity similar
to, but distinct from, PDK1.
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