Premium
Regulation of dendritic spine morphology by SPIN90, a novel Shank binding partner
Author(s) -
Kim SeonMyung,
Choi Kyu Yeong,
Cho In Ha,
Rhy Jin Hee,
Kim Sung Hyun,
Park ChulSeung,
Kim Eunjoon,
Song Woo Keun
Publication year - 2009
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.2009.06039.x
Subject(s) - dendritic spine , dendritic filopodia , postsynaptic potential , microbiology and biotechnology , excitatory postsynaptic potential , postsynaptic density , actin remodeling of neurons , actin cytoskeleton , actin , biology , spine (molecular biology) , knockout mouse , cytoskeleton , neuroscience , hippocampal formation , chemistry , inhibitory postsynaptic potential , receptor , biochemistry , cell
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.