SLK or LOSK is a Ste20-like protein kinase that associates with microtubule and centrosome. Inhibition of SLK activity by dominant-negative mutant or RNAi leads to unfocused microtubule arrangement indicating that SLK is needed for microtubule organization and for the proper localization of Golgi complex. Expression of v-Src can down-regulate SLK activity through the involvement of CK2 which can directly phosphorylate and inhibit SLK activity whereas inhibition of CK2 in v-Src-transformed cells results in normal SLK activity. CK2 and SLK can be co-localized in fibroblasts spreading on fibronectin-coated substrates.
The Journal of biological chemistry, 281(38), 28193-28199 (2006-07-14)
We have previously shown that the Ste20-like kinase SLK is a microtubule-associated protein inducing actin stress fiber disassembly. Here, we show that v-Src expression can down-regulate SLK activity. This down-regulation is independent of focal adhesion kinase but requires v-Src kinase
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