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J. Biol. Chem., Vol. 277, Issue 46, 44140-44146, November 15, 2002

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Identification of Nd1, a Novel Murine Kelch Family Protein, Involved in Stabilization of Actin Filaments^*

Kazushi Sasagawa^§, Yuji Matsudo, Myenmo Kang, Lisa Fujimura, Yoshinori Iitsuka, Seiji Okada, Takenori Ochiai^§, Takeshi Tokuhisa, and Masahiko Hatano^¶

From the  Department of Developmental Genetics (H2) and the ^§ Department of Academic Surgery (M9), Graduate School of Medicine, Chiba University, Chiba 260-8670, Japan

We isolated Nd1, a novel kelch family gene that encodes two forms of proteins, Nd1-L and Nd1-S. Nd1-L contains a BTB/POZ domain in its N terminus and six kelch repeats in the C terminus. Nd1-S has the BTB/POZ domain but lacks the six kelch repeats. Nd1-L but not Nd1-S mRNA is detected ubiquitously in normal mouse tissues. Nd1-L and Nd1-S proteins can form a dimer through the BTB/POZ domain. Nd1-L colocalizes with actin filaments detected using a confocal microscope, and its kelch repeats bind to them in vitro. Overexpression of Nd1-L in NIH3T3 cells delayed cell growth by affecting the transition of cytokinesis. Furthermore, the overexpression prevented NIH3T3 cells from cell death induced by actin destabilization but not by microtubule dysfunction. These data suggest that Nd1-L functions as a stabilizer of actin filaments as an actin-binding protein and may play a role in the dynamic organization of the actin cytoskeleton.

The nucleotide sequences for the Nd1-L and Nd1-S have been deposited in GenBank^TM under the accession numbers AB055737 and AB055738, respectively.

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