© 2005 The Japanese Biochemical Society
Regular Paper |
Phospholipase C
4 Associates with Glutamate Receptor Interacting Protein 1 in Testis
Laboratory of Genome and Biosignal, School of Life Science, Tokyo University of Pharmacy and Life Science, 1432-1 Horinouchi, Hachioji, Tokyo 192-0392
* To whom correspondence should be addressed. Tel: +81-426-76-7214; Fax: +81-426-76-7249, E-mail: kfukami{at}ls.toyaku.ac.jp
We reported previously that phospholipase C (PLC)
4 is required for calcium mobilization in the zona pellucidainduced acrosome reaction in sperm. Here we focused on the function of the C2 domain of PLC
4 and report that glutamate receptorinteracting protein1 (GRIP1) was identified as a binding protein of the PLC
4-C2 domain on yeast two-hybrid screening. Physiological interaction of GRIP1 with PLC
4 in mouse testis was confirmed by immunoprecipitation with anti-PLC
4 antibodies and the association seemed to correlate with the maturation stage of sperm. We also determined that a PDZ-binding motif at the C-terminus of the PLC
4-C2 domain is responsible for GRIP1 binding, whereas the sixth or seventh PDZ domain of GRIP1 is essential and sufficient for association with the PLC
4-C2 domain. These results indicate that PLC
4 binds via its C2 domain to the PDZ6 or PDZ7 domain of GRIP1, and that this association may play a role in spermatogenesis.