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http://dspace.mediu.edu.my:8181/xmlui/handle/10261/4820| Title: | Neurogranin binds to phosphatidic acid and associates to cellular membranes |
| Authors: | Ministerio de Ciencia y Tecnología (España) Fundación Ramón Areces Comunidad de Madrid |
| Keywords: | Calmodulin Neurogranin Phosphatidic acid Phosphatidylinositol 4,5-bisphosphate Phospholipase D (PLD), Protein kinase C (PKC) |
| Publisher: | Portland Press |
| Description: | The final version of record is available at http://dx.doi.org/10.1042/BJ20061483 Neurogranin (Ng) is a 78-amino-acid-long protein concentrated at dendritic spines of forebrain neurons that is involved in synaptic plasticity through the regulation of CaM (calmodulin)-mediated signalling. Ng features a central IQ motif that mediates binding to CaM and is phosphorylated by PKC (protein kinase C). We have analysed the subcellular distribution of Ng and found that it associates to cellular membranes in rat brain. In vitro binding assays revealed that Ng selectively binds to PA (phosphatidic acid) and that this interaction is prevented by CaM and PKC phosphorylation. Using the peptide Ng-(29–47) and a mutant with an internal deletion (Ng-IQless), we have shown that Ng binding to PA and to cellular membranes is mediated by its IQ motif. Ng expressed in NIH-3T3 cells accumulates at peripheral regions of the plasma membrane and localizes at intracellular vesicles that can be clearly visualized following saponin permeabilization. This distribution was affected by PLD (phospholipase D) and PIP5K (phosphatidylinositol 4-phosphate 5-kinase) overexpression. Based on these results, we propose that Ng binding to PA may be involved in Ng accumulation at dendritic spines and that Ng could modulate PA signalling in the postsynaptic environment. This work was supported by a grant from the Spanish Ministry of Science and Technology (BFI2002- 01581). We thank “Fundación Ramón Areces” for institutional support. Irene Domínguez-González was recipient of a fellowship from the Comunidad Autónoma de Madrid (CAM) Peer reviewed |
| URI: | http://dspace.mediu.edu.my:8181/xmlui/handle/10261/4820 |
| Other Identifiers: | Biochem. J. (2007) 404 (31–43) 0264-6021 (Print) http://hdl.handle.net/10261/4820 |
| Appears in Collections: | Digital Csic |
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