Domains, Amino Acid Residues, and New Isoforms of Caenorhabditis Elegans Diacylglycerol Kinase 1 (DGK-1) Important for Terminating Diacylglycerol Signaling in Vivo*□S
Supplemental Material can be found at: http://www.jbc.org/content/suppl/2004/12/06/M409460200.DC1.html THE JOURNAL OF BIOLOGICAL CHEMISTRY Vol. 280, No. 4, Issue of January 28, pp. 2730–2736, 2005 © 2005 by The American Society for Biochemistry and Molecular Biology, Inc. Printed in U.S.A. Domains, Amino Acid Residues, and New Isoforms of Caenorhabditis elegans Diacylglycerol Kinase 1 (DGK-1) Important for Terminating Diacylglycerol Signaling in Vivo*□S Received for publication, August 17, 2004, and in revised form, November 22, 2004 Published, JBC Papers in Press, November 24, 2004, DOI 10.1074/jbc.M409460200 Antony M. Jose‡ and Michael R. Koelle§¶ From the ‡Departments of Molecular, Cellular, and Developmental Biology and §Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, Connecticut 06520 Diacylglycerol kinases (DGKs) inhibit diacylglycerol numerous cellular processes mediated by neurotransmitters, (DAG) signaling by phosphorylating DAG. DGK-1, the growth factors, and hormones (3). DAG also activates the syn- Caenorhabditis elegans ortholog of human neuronal aptic vesicle priming protein UNC-13 (4, 5) to control neuro- DGK, inhibits neurotransmission to control behavior. transmission and certain transient receptor potential cation Downloaded from DGK-1, like DGK, has three cysteine-rich domains channels (6). In humans, nine DGK isozymes have been iden- (CRDs), a pleckstrin homology domain, and a kinase tified (DGK␣, , ␥, ␦, , ⑀, , , and ), but their physiological domain. To identify DGK domains and amino acid resi- functions remain largely unknown (1, 2). dues critical for terminating DAG signaling in vivo,we C. elegans DGK-1 provides a genetically tractable model for analyzed 20 dgk-1 mutants defective in DGK-1-con- elucidating the physiological functions of diacylglycerol ki- trolled behaviors.
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