NeuroMolecular Medicine

, Volume 2, Issue 1, pp 61–69

The actin-binding domain of spinophilin is necessary and sufficient for targeting to dendritic spines

Authors

    • Laboratory of Molecular and Cellular NeuroscienceThe Rockefeller University
  • Linda C. Hsieh-Wilson
    • Laboratory of Molecular and Cellular NeuroscienceThe Rockefeller University
    • Division of Chemistry and Chemical EngineeringCalifornia Institute of Technology
  • Patrick B. Allen
    • Laboratory of Molecular and Cellular NeuroscienceThe Rockefeller University
  • Angus C. Nairn
    • Laboratory of Molecular and Cellular NeuroscienceThe Rockefeller University
    • Department of PsychiatryYale University School of Medicine
  • Paul Greengard
    • Laboratory of Molecular and Cellular NeuroscienceThe Rockefeller University
Original Research

DOI: 10.1385/NMM:2:1:61

Cite this article as:
Grossman, S.D., Hsieh-Wilson, L.C., Allen, P.B. et al. Neuromol Med (2002) 2: 61. doi:10.1385/NMM:2:1:61

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.

Index Entries

SpinophilinNeurabin IIdendritic spinesactinpostsynaptic density

Copyright information

© Humana Press Inc 2002