Papers

Peer-reviewed Last author Corresponding author
Aug, 1999

Ca²⁺/calmodulin-dependent protein kinase cascade in Caenorhabditis elegans - Implication in transcriptional activation

The Journal of Biological Chemistry
  • Koh Eto
  • ,
  • Naomi Takahashi
  • ,
  • Yoshishige Kimura
  • ,
  • Yasuhiko Masuho
  • ,
  • Ken-ichi Arai
  • ,
  • Masa-aki Muramatsu
  • ,
  • Hiroshi Tokumitsu

Volume
274
Number
32
First page
22556
Last page
22562
Language
English
Publishing type
Research paper (scientific journal)
Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC

We have recently demonstrated that Caenorhabditis elegans Ca2+/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. Ce-CaM-KI has 348 amino acid residues with an apparent molecular mass of 40 kDa, which is activated by Ce-CaM-KK through phosphorylation of Thr(179) 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-RI, CeCaM-KI is mainly localized in the nucleus of transfected cells because the NH2-terminal six residues ((PLFKRR7)-P-2) contain a functional nuclear localization signal. We have also demonstrated that CeCaM-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 Ce-CaM-KI. These results suggest that the CaM-KK/CaM-KI cascade is conserved in C. 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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Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000081868400063&DestApp=WOS_CPL
ID information
  • ISSN : 0021-9258
  • Web of Science ID : WOS:000081868400063

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