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Ca2+/Calmodulin-dependent Protein Kinase Cascade in Caenorhabditis elegans

Koh Eto,Naomi Takahashi,Yoshishige Kimura,Yasuhiko Masuho,Ken-ichi Arai,Masa-aki Muramatsu,H. Tokumitsu

Published 1999 in Journal of Biological Chemistry

ABSTRACT

We have recently demonstrated thatCaenorhabditis elegansCa2+/calmodulin-dependent protein kinase kinase (CeCaM-KK) can activate mammalian CaM-kinase IV in vitro (Tokumitsu, H., Takahashi, N., Eto, K., Yano, S., Soderling, T.R., and Muramatsu, M. (1999) J. Biol. Chem. 274, 15803–15810). In the present study, we have identified and cloned a target CaM-kinase for CaM-KK in C. elegans, CeCaM-kinase I (CeCaM-KI), which has approximately 60% identity to mammalian CaM-KI.CeCaM-KI has 348 amino acid residues with an apparent molecular mass of 40 kDa, which is activated by CeCaM-KK through phosphorylation of Thr179 in a Ca2+/CaM-dependent manner, resulting in a 30-fold decrease in the K m of CeCaM-KI for its peptide substrate. Unlike mammalian CaM-KI,CeCaM-KI is mainly localized in the nucleus of transfected cells because the NH2-terminal six residues (2PLFKRR7) contain a functional nuclear localization signal. We have also demonstrated thatCeCaM-KK and CeCaM-KI reconstituted a signaling pathway that mediates Ca2+-dependent phosphorylation of cAMP response element-binding protein (CREB) and CRE-dependent transcriptional activation in transfected cells, consistent with nuclear localization of CeCaM-KI. These results suggest that the CaM-KK/CaM-KI cascade is conserved inC. elegans and is functionally operated both in vitro and in intact cells, and it may be involved in Ca2+-dependent nuclear events such as transcriptional activation through phosphorylation of CREB.

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