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J. Cell Biol.,
Volume 139, Number 4, November 17, 1997 951-961
* Takai Biotimer Project, ERATO, Japan Science and Technology Corporation, c/o JCR Pharmaceuticals Co., Ltd., Nishi-ku,
Kobe 651-22, Japan; We purified from rat brain a novel actin filament (F-actin)-binding protein of ~180 kD (p180),
which was specifically expressed in neural tissue. We
named p180 neurabin (neural tissue-specific F-actin-
binding protein). We moreover cloned the cDNA of
neurabin from a rat brain cDNA library and characterized native and recombinant proteins. Neurabin was a
protein of 1,095 amino acids with a calculated molecular mass of 122,729. Neurabin had one F-actin-binding
domain at the NH2-terminal region, one PSD-95, DlgA,
ZO-1-like domain at the middle region, a domain
known to interact with transmembrane proteins, and
domains predicted to form coiled-coil structures at the
COOH-terminal region. Neurabin bound along the
sides of F-actin and showed F-actin-cross-linking activity. Immunofluorescence microscopic analysis revealed
that neurabin was highly concentrated in the synapse of
the developed neurons. Neurabin was also concentrated in the lamellipodia of the growth cone during the
development of neurons. Moreover, a study on suppression of endogenous neurabin in primary cultured
rat hippocampal neurons by treatment with an antisense oligonucleotide showed that neurabin was involved in the neurite formation. Neurabin is a candidate for key molecules in the synapse formation and
function.
Department of Molecular Biology and Biochemistry, Osaka University Medical School, Suita 565, Japan; § Department of Virology II, National Institutes of Health, Tokyo 162, Japan; Department of Anatomy and Neurobiology,
Graduate School, Kyoto University, Kyoto 606-01, Japan
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