Actin-binding proteins in a postsynaptic preparation: Lasp-1 is a component of central nervous system synapses and dendritic spines

J Neurosci Res. 2004 Oct 1;78(1):38-48. doi: 10.1002/jnr.20224.

Abstract

CNS synapses are complex sites of cell-cell communication. Identification and characterization of the protein components of synapses will lead to a better understanding of the mechanisms of neurotransmission and plasticity. We applied multidimensional protein identification technology (MudPIT) to purified, guanidine-solubilized postsynaptic fractions to identify novel synaptically localized molecules. We identified several actin-associated proteins known to regulate actin polymerization and control cell motility in nonneural cells that have not previously been associated with CNS synaptic function. One of these is lasp-1, an actin-associated LIM and SH3 domain-containing protein. We show that lasp-1 is strongly expressed by CNS neurons and is concentrated at synaptic sites. Overall, the preponderance of actin-associated proteins in postsynaptic density fractions, and specifically those involved in actin reorganization, suggests that there are many modes by which the state of synaptic F-actin polymerization and, hence, synaptic physiology are affected.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Actins / metabolism*
  • Adaptor Proteins, Signal Transducing
  • Animals
  • Brain / metabolism*
  • Brain / ultrastructure
  • Cells, Cultured
  • Cytoskeletal Proteins
  • DNA, Protozoan
  • Dendrites / chemistry
  • Dendrites / metabolism*
  • Dendrites / ultrastructure
  • Homeodomain Proteins / biosynthesis
  • Homeodomain Proteins / metabolism
  • Homeodomain Proteins / ultrastructure
  • LIM Domain Proteins
  • Male
  • Microfilament Proteins / biosynthesis
  • Microfilament Proteins / metabolism*
  • Microfilament Proteins / ultrastructure
  • Neoplasm Proteins / biosynthesis
  • Neoplasm Proteins / metabolism
  • Neoplasm Proteins / ultrastructure
  • Nerve Tissue Proteins / biosynthesis
  • Nerve Tissue Proteins / metabolism*
  • Nerve Tissue Proteins / ultrastructure
  • Rats
  • Rats, Sprague-Dawley
  • Synaptic Membranes / chemistry
  • Synaptic Membranes / metabolism*
  • Synaptic Membranes / ultrastructure

Substances

  • Actins
  • Adaptor Proteins, Signal Transducing
  • Cytoskeletal Proteins
  • DNA, Protozoan
  • Homeodomain Proteins
  • LASP1 protein, human
  • LIM Domain Proteins
  • Lasp1 protein, rat
  • Microfilament Proteins
  • Neoplasm Proteins
  • Nerve Tissue Proteins