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Molecular and Cellular Biology, October 2003, p. 7329-7338, Vol. 23, No. 20
0270-7306/03/$08.00+0     DOI: 10.1128/MCB.23.20.7329-7338.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Role of Phospholipase C-L2, a Novel Phospholipase C-Like Protein That Lacks Lipase Activity, in B-Cell Receptor Signaling

Kei Takenaka,1 Kiyoko Fukami,1,2 Makiko Otsuki,1 Yoshikazu Nakamura,1 Yuki Kataoka,3 Mika Wada,4 Kohichiro Tsuji,4 Shin-Ichi Nishikawa,5 Nobuaki Yoshida,3 and Tadaomi Takenawa1,2*

Department of Biochemistry,1 Division of Gene Expression and Regulation,3 Division of Cellular Therapy, The Institute of Medical Science, University of Tokyo, Tokyo 108-8639,4 Department of Molecular Genetics, Kyoto University Graduate School of Medicine, Kyoto 606-8509,5 Core Research for Evolutional Science and Technology of Japan Science and Technology Corporation, Honcho, Kawaguchi City, Saitama Prefecture 332-0012, Japan2

Received 16 April 2003/ Returned for modification 12 June 2003/ Accepted 30 June 2003

Phospholipase C (PLC) plays important roles in phosphoinositide turnover by regulating the calcium-protein kinase C signaling pathway. PLC-L2 is a novel PLC-like protein which lacks PLC activity, although it is very homologous with PLC {delta}. PLC-L2 is expressed in hematopoietic cells, but its physiological roles and intracellular functions in the immune system have not yet been clarified. To elucidate the physiological function of PLC-L2, we generated mice which had a genetic PLC-L2 deficiency. PLC-L2-deficient mice grew with no apparent abnormalities. However, mature B cells from PLC-L2-deficient mice were hyperproliferative in response to B-cell receptor (BCR) cross-linking, although B2 cell development appeared to be normal. Molecular biological analysis revealed that calcium influx and NFATc accumulation in nuclei were increased in PLC-L2-deficient B cells. Extracellular signal-regulated kinase activity was also enhanced in PLC-L2-deficient B cells. These mice had a stronger T-cell-independent antigen response. These results indicate that PLC-L2 is a novel negative regulator of BCR signaling and immune responses.

* Corresponding author. Mailing address: Department of Biochemistry, The Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minatoku, Tokyo 108-8639, Japan. Phone: 81-3-5449-5510. Fax: 81-3-5449-5417. E-mail: takenawa{at}ims.u-tokyo.ac.jp.

Molecular and Cellular Biology, October 2003, p. 7329-7338, Vol. 23, No. 20
0022-538X/03/$08.00+0     DOI: 10.1128/MCB.23.20.7329-7338.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Mizokami, A., Kanematsu, T., Ishibashi, H., Yamaguchi, T., Tanida, I., Takenaka, K., Nakayama, K. I., Fukami, K., Takenawa, T., Kominami, E., Moss, S. J., Yamamoto, T., Nabekura, J., Hirata, M. (2007). Phosholipase C-Related Inactive Protein Is Involved in Trafficking of {gamma}2 Subunit-Containing GABAA Receptors to the Cell Surface. J. Neurosci. 27: 1692-1701 [Abstract] [Full Text]  
  • Kanematsu, T., Yasunaga, A., Mizoguchi, Y., Kuratani, A., Kittler, J. T., Jovanovic, J. N., Takenaka, K., Nakayama, K. I., Fukami, K., Takenawa, T., Moss, S. J., Nabekura, J., Hirata, M. (2006). Modulation of GABAA Receptor Phosphorylation and Membrane Trafficking by Phospholipase C-related Inactive Protein/Protein Phosphatase 1 and 2A Signaling Complex Underlying Brain-derived Neurotrophic Factor-dependent Regulation of GABAergic Inhibition. J. Biol. Chem. 281: 22180-22189 [Abstract] [Full Text]  


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