TY - JOUR
T1 - Direct interaction of GluRδ2 with Shank scaffold proteins in cerebellar Purkinje cells
AU - Uemura, Takeshi
AU - Mori, Hisashi
AU - Mishina, Masayoshi
N1 - Funding Information:
We thank Dr. Masahiko Watanabe for antibodies against GluRδ2, GluRε1, PSD-93, and PSD-95, Drs Hidemi Shimizu and. Masahiko Watanabe for anti-calbindin antibody, Dr. Yutaka Hata for anti-Synamon antibody, Dr. Susumu Kawamoto for anti-Delphilin antibody, Dr. Kenji Sakimura for anti-GRIP1 antibody, and Dr. Tobias M. Boeckers for anti-ProSAP1 antibody. We are also grateful to Dr. Akiko Fujiwara and Mr. Yohei Okubo for advice on cerebellar culture and Ms. Yumiko Nakjima for help in the preparation of manuscript. This work was supported in part by research grants from the Japan Science and Technology Corporation and the Ministry of Education, Culture, Sports, Science and Technology of Japan.
PY - 2004/6
Y1 - 2004/6
N2 - Glutamate receptor (GluR) δ2 selectively expressed in cerebellar Purkinje cells plays a central role in cerebellar long-term depression (LTD), motor learning, and formation of parallel fiber synapses. By yeast two-hybrid screening, we identified members of the Shank family of scaffold proteins as major GluRδ2-interacting molecules. GluRδ2 bound directly to the PDZ domain of Shank proteins through an internal motif in the carboxyl-terminal putative cytoplasmic domain. Shank1 and Shank2 proteins as well as GluRδ2 proteins were localized in the dendritic spines of cultured Purkinje cells. Anti-GluRδ2 antibodies immunoprecipitated Shank1, Shank2, Homer, and metabotropic GluR1α proteins from the synaptosomal membrane fractions of cerebella. Furthermore, Shank2 interacted with GRIP1 in the cerebellum. These results suggest that through Shank1 and Shank2, GluRδ2 interacts with the metabotropic GluR1α, the AMPA-type GluR, and the inositol 1,4,5-trisphosphate receptor (IP3R) that are essential for cerebellar LTD.
AB - Glutamate receptor (GluR) δ2 selectively expressed in cerebellar Purkinje cells plays a central role in cerebellar long-term depression (LTD), motor learning, and formation of parallel fiber synapses. By yeast two-hybrid screening, we identified members of the Shank family of scaffold proteins as major GluRδ2-interacting molecules. GluRδ2 bound directly to the PDZ domain of Shank proteins through an internal motif in the carboxyl-terminal putative cytoplasmic domain. Shank1 and Shank2 proteins as well as GluRδ2 proteins were localized in the dendritic spines of cultured Purkinje cells. Anti-GluRδ2 antibodies immunoprecipitated Shank1, Shank2, Homer, and metabotropic GluR1α proteins from the synaptosomal membrane fractions of cerebella. Furthermore, Shank2 interacted with GRIP1 in the cerebellum. These results suggest that through Shank1 and Shank2, GluRδ2 interacts with the metabotropic GluR1α, the AMPA-type GluR, and the inositol 1,4,5-trisphosphate receptor (IP3R) that are essential for cerebellar LTD.
UR - http://www.scopus.com/inward/record.url?scp=2942689457&partnerID=8YFLogxK
U2 - 10.1016/j.mcn.2004.02.007
DO - 10.1016/j.mcn.2004.02.007
M3 - 学術論文
C2 - 15207857
AN - SCOPUS:2942689457
SN - 1044-7431
VL - 26
SP - 330
EP - 341
JO - Molecular and Cellular Neuroscience
JF - Molecular and Cellular Neuroscience
IS - 2
ER -