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Regulation of dendritic spine morphology by SPIN90, a novel Shank binding partner |
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| Authors: | Seon-Myung Kim Kyu Yeong Choi† In Ha Cho Jin Hee Rhy Sung Hyun Kim‡ Chul-Seung Park Eunjoon Kim§ Woo Keun Song |
| Institution: | Cell Dynamics Research Center and Bioimaging Center, Gwangju Institute of Science and Technology, Gwangju, Korea; National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland, USA; Department of Biochemistry, Weill Medical College of Cornell University, New York, New York, USA; Department of Biological Sciences, National Creative Research Initiative Center for Synaptogenesis, Korea Advanced Institute of Science and Technology, Daejeon, Korea |
| Abstract: | Dendritic spines are highly specialized actin-rich structures on which the majority of excitatory synapses are formed in the mammalian CNS. SPIN90 is an actin-binding protein known to be highly enriched in postsynaptic densities (PSDs), though little is known about its function there. Here, we show that SPIN90 is a novel binding partner for Shank proteins in the PSD. SPIN90 and Shank co-immunoprecipitate from brain lysates and co-localize in postsynaptic dendrites and act synergistically to mediate spine maturation and spine head enlargement. At the same time, SPIN90 causes accumulation of Shank and PSD-95 within dendritic spines. In addition, we found that the protein composition of PSDs in SPIN90 knockout mice is altered as is the actin cytoskeleton of cultured hippocampal SPIN90 knockout neurons. Taken together, these findings demonstrate that SPIN90 is a Shank1b binding partner and a key contributor to the regulation of dendritic spine morphogenesis and brain function. |
| Keywords: | cytoskeleton dendritic spines hippocampus postsynaptic density scaffolding protein |