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The Journal of Neuroscience, October 1, 1999, 19(19):8389-8400
Cupidin, an Isoform of Homer/Vesl, Interacts with the Actin
Cytoskeleton and Activated Rho Family Small GTPases and Is Expressed in
Developing Mouse Cerebellar Granule Cells
Yoko
Shiraishi1, 2, 3,
Akihiro
Mizutani1, 3,
Haruhiko
Bito4,
Kazuko
Fujisawa4,
Shuh
Narumiya4,
Katsuhiko
Mikoshiba1, 3, and
Teiichi
Furuichi1, 2
1 Department of Molecular Neurobiology, Institute of
Medical Science, The University of Tokyo, Minato-ku, Tokyo
108-8639 , Japan, 2 Laboratory for Molecular
Neurogenesis and 3 Developmental Neurobiology, Brain
Science Institute, The Institute of Physical and Chemical Research
(RIKEN), Wako, Saitama 351-0198, Japan, and 4 Department of
Pharmacology, Kyoto University Faculty of Medicine, Sakyo-ku, Kyoto
606-8315, Japan
A developmentally regulated Homer/Vesl isoform, Cupidin (Homer
2a/Vesl-2 11), was isolated from postnatal mouse cerebellum using a
fluorescent differential display strategy. The strongest expression of
Cupidin was detected in the cerebellar granule cells at approximately
postnatal day 7. Cupidin was enriched in the postsynaptic
density fraction, and its immunoreactivity was concentrated at
glomeruli of the inner granular layer when active synaptogenesis occurred. Cupidin protein could be divided into two functional domains:
the N-terminal portion, which was highly conserved among Homer/Vesl
family proteins, and the C-terminal portion, which consisted of a
putative coiled-coil structure, including several leucine zipper
motifs. The N-terminal fragment of Cupidin, which was able to associate
with metabotropic glutamate receptor 1 (mGluR1), also interacted with
F-actin in vitro. In keeping with this, F-actin immunocytochemically colocalized with Cupidin in cultured cerebellar granule cells, and a Cupidin-mGluR1-actin complex was
immunoprecipitated from crude cerebellar lysates using an anti-Cupidin
antibody. On the other hand, the C-terminal portion of Cupidin bound to Cdc42, a member of Rho family small GTPases, in a GTP-dependent manner
in vitro, and Cupidin functionally interacted with
activated-Cdc42 in a heterologous expression system. Together, our
findings indicate that Cupidin may serve as a postsynaptic scaffold
protein that links mGluR signaling with actin cytoskeleton and Rho
family proteins, perhaps during the dynamic phase of morphological
changes that occur during synapse formation in cerebellar granule cells.
Key words:
Cupidin/Homer 2a/Vesl-211; cerebellar development; granule cell; mGluR; actin cytoskeleton; Rho family small GTPases
Copyright © 1999 Society for Neuroscience 0270-6474/99/19198389-12$05.00/0
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