The actin-binding domain of spinophilin is necessary and sufficient for targeting to dendritic spines
Abstract
Spinophilin is enriched in dendritic spines, small protrusions of the postsynaptic membrane along the length of the dendrite that contain the majority of excitatory synapses. Spinophilin binds to protein phosphatase 1 with high affinity and targets it to dendritic spines, therefore placing it in proximity to regulate glutamate receptor activity. Spinophilin also binds to and bundles f-actin, the main cytoskeletal constituent of dendritic spines, and may therefore serve to regulate the structure of the synapse. In this study, we sought to determine the structural basis for the targeting of spinophilin to dendritic spines. Our results show that the actin-binding domain of spinophilin is necessary and sufficient for targeting of spinophilin to dendrites and dendritic spines.
Additional Information
© 2002 Humana Press Inc. Received April 23, 2002; Accepted May 21, 2002. This research was supported by funding from The Rockefeller University's Women & Science Fellowship Program (to S.D.G.), The National Alliance for Research on Schizophrenia and Depression (to S.D.G.), NIMH grant 2T32MH15125 (S.D.G.), and by U.S.P.H.S. grants MH 40899 and DA10044 (P.G.& A.C.N.). We thank Dr. Sanford Simon for technical assistance.Additional details
- Eprint ID
- 57667
- Resolver ID
- CaltechAUTHORS:20150519-135757138
- Rockefeller University's Women & Science Fellowship Program
- National Alliance for Research on Schizophrenia and Depression
- 2T32MH15125
- NIH Predoctoral Fellowship
- MH40899
- NIH
- DA10044
- NIH
- Created
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2015-05-19Created from EPrint's datestamp field
- Updated
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2021-11-10Created from EPrint's last_modified field