期刊
JOURNAL OF NEUROSCIENCE
卷 28, 期 41, 页码 10220-10233出版社
SOC NEUROSCIENCE
DOI: 10.1523/JNEUROSCI.3434-08.2008
关键词
motor neurons; spinal cord; synaptic activity; postsynaptic density; trafficking; scaffold protein
资金
- Howard Hughes Medical Institute Funding Source: Medline
- NINDS NIH HHS [R01 NS036715, R01 NS029837, R01 NS036715-08, NS 52325, NS 29837] Funding Source: Medline
Activity-dependent dendrite elaboration influences the pattern of interneuronal connectivity and network function. In the present study, we examined the mechanism by which the GluR1 subunit of AMPA receptors controls dendrite morphogenesis. GluR1 binds to SAP97, a scaffolding protein that is a component of the postsynaptic density, via its C-terminal 7aa. We find that elimination of this interaction in vitro or in vivo by deleting the C-terminal 7 aa of GluR1, GluR1 Delta 7) does not influence trafficking, processing, or cell surface GluR1 expression but does prevent translocation of SAP97 from the cytosol to membranes. GluR1 and SAP97 together at the plasma membrane promotes dendrite branching in an activity-dependent manner, although this does not require physical association. Our findings suggest that the C-terminal 7 aa of GluR1 are essential for bringing SAP97 to the plasma membrane, where it acts to translate the activity of AMPA receptors into dendrite growth.
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