Role of Septin cytoskeleton in spine morphogenesis and dendrite development in neurons.

@article{citeulike:2737420, abstract = {Septins are GTP-binding proteins that polymerize into heteromeric filaments and form microscopic bundles or ring structures in vitro and in vivo. Because of these properties and their ability to associate with membrane, F-actin, and microtubules, septins have been generally regarded as cytoskeletal components [1, 2]. Septins are known to play roles in cytokinesis, in membrane trafficking, and as structural scaffolds; however, their function in neurons is poorly understood. Many members of the septin family, including Septin 7 (Sept7), were found by mass-spectrometry analysis of postsynaptic density (PSD) fractions of the brain [3, 4], suggesting a possible postsynaptic function of septins in neurons. We report that Sept7 is localized at the base of dendritic protrusions and at dendritic branch points in cultured hippocampal neurons--a distribution reminiscent of septin localization in the bud neck of budding yeast. Overexpression of Sept7 increased dendrite branching and the density of dendritic protrusions, whereas RNA interference (RNAi)-mediated knockdown of Sept7 led to reduced dendrite arborization and a greater proportion of immature protrusions. These data suggest that Sept7 is critical for spine morphogenesis and dendrite development during neuronal maturation.}, address = {The Picower Institute for Learning and Memory, RIKEN-MIT Neuroscience Research Center, Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.}, author = {Tada, T. and Simonetta, A. and Batterton, M. and Kinoshita, M. and Edbauer, D. and Sheng, M. }, citeulike-article-id = {2737420}, doi = {10.1016/j.cub.2007.09.039}, issn = {0960-9822}, journal = {Current biology : CB}, keywords = {cytosqueleton, dendritic\_spines, neurites\_growth}, month = {October}, number = {20}, pages = {1752--1758}, posted-at = {2008-04-30 10:55:27}, priority = {0}, title = {Role of Septin cytoskeleton in spine morphogenesis and dendrite development in neurons.}, url = {http://dx.doi.org/10.1016/j.cub.2007.09.039}, volume = {17}, year = {2007} }

TY - JOUR ID - citeulike:2737420 TI - Role of Septin cytoskeleton in spine morphogenesis and dendrite development in neurons. JF - Current biology : CB VL - 17 IS - 20 SP - 1752 EP - 1758 AD - The Picower Institute for Learning and Memory, RIKEN-MIT Neuroscience Research Center, Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA. SN - 0960-9822 N2 - Septins are GTP-binding proteins that polymerize into heteromeric filaments and form microscopic bundles or ring structures in vitro and in vivo. Because of these properties and their ability to associate with membrane, F-actin, and microtubules, septins have been generally regarded as cytoskeletal components [1, 2]. Septins are known to play roles in cytokinesis, in membrane trafficking, and as structural scaffolds; however, their function in neurons is poorly understood. Many members of the septin family, including Septin 7 (Sept7), were found by mass-spectrometry analysis of postsynaptic density (PSD) fractions of the brain [3, 4], suggesting a possible postsynaptic function of septins in neurons. We report that Sept7 is localized at the base of dendritic protrusions and at dendritic branch points in cultured hippocampal neurons--a distribution reminiscent of septin localization in the bud neck of budding yeast. Overexpression of Sept7 increased dendrite branching and the density of dendritic protrusions, whereas RNA interference (RNAi)-mediated knockdown of Sept7 led to reduced dendrite arborization and a greater proportion of immature protrusions. These data suggest that Sept7 is critical for spine morphogenesis and dendrite development during neuronal maturation. KW - cytosqueleton KW - dendritic_spines KW - neurites_growth AU - Tada, T AU - Simonetta, A AU - Batterton, M AU - Kinoshita, M AU - Edbauer, D AU - Sheng, M PY - 2007/10/23/ UR - http://dx.doi.org/10.1016/j.cub.2007.09.039 ER -