TI  - Competitive binding of  <prot>alpha-actinin</prot>  and  <prot>calmodulin</prot>  to the   <prot>NMDA receptor</prot>  .
PG  - 439-42
AB  - The mechanisms by which neurotransmitter receptors are immobilized at
      postsynaptic sites in neurons are largely unknown. The activity of NMDA
      (N-methyl-D-aspartate) receptors is mechanosensitive and dependent on the
      integrity of <prot>actin</prot>, suggesting a functionally important interaction
      between NMDA receptors and the postsynaptic cytoskeleton.   <prot>alpha-Actinin-2</prot>  ,
      a member of the spectrin/<prot>dystrophin</prot> family of <prot>actin</prot>-binding proteins, is
      identified here as a brain postsynaptic density protein that colocalizes
      in dendritic spines with  NMDA receptors  and the putative NMDA
      receptor-clustering molecule  <prot>PSD-95</prot> . <prot>alpha-Actinin-2</prot>   binds by its central
      rod domain to the cytoplasmic tail of both <prot>NR1</prot> and <prot>NR2B</prot> subunits of the
       <prot>NMDA receptor</prot> , and can be immunoprecipitated with NMDA receptors and
      <prot>PSD-95</prot> from rat brain. Intriguingly,  <prot>NR1</prot> - <prot>alpha-actinin</prot>  binding is directly
      antagonized by Ca2+/<prot>calmodulin</prot>. Thus <prot>alpha-actinin</prot> may play a role in both
      the localization of NMDA receptors and their modulation by Ca2+.
AD  - Howard Hughes Medical Institute, Harvard Medical School, Boston,
