CIP98, a novel PDZ domain protein, is expressed in the central nervous system and interacts with calmodulin-dependent serine kinase. Export

@article{citeulike:5950210, abstract = {Receptors and various molecules in neurons are localized at precise locations to perform their respective functions, especially in synaptic sites. Among synaptic molecules, PDZ domain proteins play major roles in scaffolding and anchoring membrane proteins for efficient synaptic transmission. In the present study, we isolated CIP98, a novel protein (98 kDa) consisting of three PDZ domains and a proline-rich region, which is widely expressed in the central nervous system. In situ hybridization and immunohistochemical staining patterns demonstrate that CIP98 is expressed strongly in certain types of neurons, i.e. pyramidal cells in layers III-V of the cerebral cortex, projecting neurons in the thalamus and interneurons in the cerebellum. The results of immunocytochemical staining and electron microscopy revealed that CIP98 is localized both in dendrites and axons. Interestingly, CIP98 interacts with CASK (calmodulin-dependent serine kinase), a member of the membrane-associated guanylate kinase (MAGUK) family that plays important roles in the molecular organization of proteins at synapses. CIP98 was shown to co-localize with CASK along the dendritic processes of neurons. In view of its direct association with CASK, CIP98 may be involved in the formation of CASK scaffolding proteins complex to facilitate synaptic transmission in the CNS.}, author = {Yap, Chan Choo C. and Liang, Fengyi and Yamazaki, Yasuhiro and Muto, Yuko and Kishida, Haruo and Hayashida, Tsuyako and Hashikawa, Tsutomu and Yano, Ryoji}, citeulike-article-id = {5950210}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/12641734}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=12641734}, issn = {0022-3042}, journal = {Journal of neurochemistry}, keywords = {calmodulin, cip98, membrane, pdz, protocol}, month = {April}, number = {1}, pages = {123--134}, posted-at = {2009-10-16 10:48:49}, priority = {2}, title = {CIP98, a novel PDZ domain protein, is expressed in the central nervous system and interacts with calmodulin-dependent serine kinase.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/12641734}, volume = {85}, year = {2003} }

TY - JOUR ID - citeulike:5950210 L3 - citeulike-article-id:5950210 N2 - Receptors and various molecules in neurons are localized at precise locations to perform their respective functions, especially in synaptic sites. Among synaptic molecules, PDZ domain proteins play major roles in scaffolding and anchoring membrane proteins for efficient synaptic transmission. In the present study, we isolated CIP98, a novel protein (98 kDa) consisting of three PDZ domains and a proline-rich region, which is widely expressed in the central nervous system. In situ hybridization and immunohistochemical staining patterns demonstrate that CIP98 is expressed strongly in certain types of neurons, i.e. pyramidal cells in layers III-V of the cerebral cortex, projecting neurons in the thalamus and interneurons in the cerebellum. The results of immunocytochemical staining and electron microscopy revealed that CIP98 is localized both in dendrites and axons. Interestingly, CIP98 interacts with CASK (calmodulin-dependent serine kinase), a member of the membrane-associated guanylate kinase (MAGUK) family that plays important roles in the molecular organization of proteins at synapses. CIP98 was shown to co-localize with CASK along the dendritic processes of neurons. In view of its direct association with CASK, CIP98 may be involved in the formation of CASK scaffolding proteins complex to facilitate synaptic transmission in the CNS. IS - 1 JF - Journal of neurochemistry SN - 0022-3042 EP - 134 TI - CIP98, a novel PDZ domain protein, is expressed in the central nervous system and interacts with calmodulin-dependent serine kinase. VL - 85 SP - 123 KW - calmodulin KW - cip98 KW - membrane KW - pdz KW - protocol AU - Yap, Chan Choo AU - Liang, Fengyi AU - Yamazaki, Yasuhiro AU - Muto, Yuko AU - Kishida, Haruo AU - Hayashida, Tsuyako AU - Hashikawa, Tsutomu AU - Yano, Ryoji PY - 2003/04// UR - http://view.ncbi.nlm.nih.gov/pubmed/12641734 ER -