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J. Biol. Chem. 276 (4): 2752-2757

© 2001 by The American Society for Biochemistry and Molecular Biology, Inc.

Regulation of a Novel Human Phospholipase C, PLCepsilon , through Membrane Targeting by Ras*

Chunhua SongDagger §, Chang-Deng HuDagger §, Misa MasagoDagger , Ken-ichi Kariya, Yuriko Yamawaki-KataokaDagger , Mitsushige ShibatohgeDagger , Dongmei WuDagger , Takaya SatohDagger , and Tohru KataokaDagger ||

From the Dagger  Department of Physiology II, Kobe University School of Medicine, 7-5-1 Kusunoki-cho, Chuo-ku, Kobe 650-0017, Japan and the  Department of Biochemistry II, School of Medicine, University of the Ryukyus, 207 Uehara, Nishihara-cho, Okinawa 903-0215, Japan

Phosphoinositide-specific phospholipase C (PI-PLC) plays a pivotal role in regulation of intracellular signal transduction from various receptor molecules. More than 10 members of human PI-PLC isoforms have been identified and classified into three classes beta , gamma , and delta , which are regulated by distinct mechanisms. Here we report identification of a novel class of human PI-PLC, named PLCepsilon , which is characterized by the presence of a Ras-associating domain at its C terminus and a CDC25-like domain at its N terminus. The Ras-associating domain of PLCepsilon specifically binds to the GTP-bound forms of Ha-Ras and Rap1A. The dissociation constant for Ha-Ras is estimated to be approximately 40 nM, comparable with those of other Ras effectors. Co-expression of an activated Ha-Ras mutant with PLCepsilon induces its translocation from the cytosol to the plasma membrane. Upon stimulation with epidermal growth factor, similar translocation of ectopically expressed PLCepsilon is observed, which is inhibited by co-expression of dominant-negative Ha-Ras. Furthermore, using a liposome-based reconstitution assay, it is shown that the phosphatidylinositol 4,5-bisphosphate-hydrolyzing activity of PLCepsilon is stimulated in vitro by Ha-Ras in a GTP-dependent manner. These results indicate that Ras directly regulates phosphoinositide breakdown through membrane targeting of PLCepsilon .

* This work was supported by Ministry of Education, Science, Sports and Culture of Japan Grants 11470034, 12215098, 12670116, and 12670136 and by funds from the Sankyo Foundation of Life Science, Hyogo Science and Technology Association, and Kobe University.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF190642.

§ These authors contributed equally to this work.

|| To whom correspondence should be addressed. Tel.: 81-78-382-5380; Fax: 81-78-382-5399; E-mail: kataoka@kobe-u.ac.jp.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.

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