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The Journal of Neuroscience, January 15, 2001, 21(2):423-433
Densin-180 Forms a Ternary Complex with the  -Subunit of
Ca2+/Calmodulin-Dependent Protein Kinase II and
-Actinin
Randall S.
Walikonis,
Asako
Oguni,
Eugenia M.
Khorosheva,
Chung-Jiuan
Jeng,
Franklin J.
Asuncion, and
Mary B.
Kennedy
Division of Biology, California Institute of Technology, Pasadena,
California 91125
Densin-180 is a transmembrane protein that is tightly associated
with the postsynaptic density in CNS neurons and is postulated to
function as a synaptic adhesion molecule. Here we report the identification of the  -subunit of
Ca2+/calmodulin-dependent protein kinase II (CaMKII)
and -actinin-4 as potential binding partners for the
densin-180 intracellular segment. We demonstrate by yeast
two-hybrid and biochemical assays that the intracellular portion of
densin-180, the -subunit of CaMKII (CaMKII), and -actinin
interact with each other at distinct binding sites and can form a
ternary complex stabilized by multiple interactions. Densin-180 binds
specifically to the association domain of CaMKII and does not bind
with high affinity to holoenzymes of CaMKII that contain  -subunit.
The PDZ (PSD-95, DIg, Z0-1) domain of densin contributes to its
binding to -actinin. A distinct domain of -actinin interacts with
the kinase domains of both - and -subunits of CaMKII.
Autophosphorylation of CaMKII increases its affinity for densin-180
from an EC50 of >1 µm to an EC50 of <75-150 nM. In contrast, phosphorylation of densin-180 by CaMKII at
serine-1397 only slightly decreases its affinity for CaMKII. The
specific interaction of densin-180 with holoenzymes of CaMKII containing only -subunit and the increased affinity of CaMKII for
densin-180 after autophosphorylation suggest that densin-180 may be
involved in localization of activated CaMKII synthesized in dendrites.
Key words:
postsynaptic density; synaptic plasticity; protein
phosphorylation; synapse; spine; neuronal cytoskeleton
Copyright © 2001 Society for Neuroscience 0270-6474/01/212423-11$05.00/0
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