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J. Biochem, 1997, Vol. 122, No. 3 525-530
© 1997 Japanese Biochemical Society


research-article

Identification and Subcellular Localization of a Novel Mammalian Dynamin-Related Protein Homologous to Yeast Vps1p and Dnm1p1

Hye-Won Shin*, Chisa Shinotsuka*, Seiji Torii{dagger},2, Kazuo Murakami{dagger},{ddagger} and Kazuhisa Nakayama*,§,3

*Institute of Biological Sciences University of Tsukuba Tsukuba Science City, Ibaraki 305
{dagger}Institute of Applied Biochemistry University of Tsukuba Tsukuba Science City, Ibaraki 305
{ddagger}Tsukuba Advanced Research Alliance Center University of Tsukuba Tsukuba Science City, Ibaraki 305
§Gene Experiment Center, University of Tsukuba Tsukuba Science City, Ibaraki 305

3 To whom correspondence should be addressed at: Institute of Biological Sciences, University of Tsukuba, Tsukuba Science City, Ibaraki 305. Tel: +81-298-53-6005, Fax: +81-298-53-6006, E-mail: kazunaka{at}sakura.cc.tsukuba.ac.jp

The dynamin family of GTP-binding proteins are implicated in vesicular transport. These include mammalian dynamins I, II, III, and yeast Vps1p and Dnm1p. Dynamin is involved in the formation of clathrin-coated vesicles at the plasma membrane. On the other hand, Vps1p and Dnmlp appear to be involved in transport from the late Golgi compartment to vacuoles and in an endocytic process, respectively. In this study, we identified a novel human protein, named Dnm1p/Vps1p-like protein (DVLP). It resembled more closely Dnmlp and Vps1p than dynamins not only in the primary structure but also in the domain organization. DVLP mRNA was expressed ubiquitously, suggesting that this protein plays a fundamental role in cellular function. Immunofluorescence analysis of cells expressing epitope-tagged DVLP revealed that it showed a diffused perinuclear staining pattern that was not superimposed on that of the marker protein for the Golgi apparatus, trans-Golgi network, lysosomes, endosomes, or endoplasmic reticulum. These data suggest that DVLP is not involved in the formation of known coated vesicles.

1This work was supported in part by grants from the Ministry of Education, Science, Sports and Culture of Japan, the University of Tsukuba Research Projects, the Special Research Project on Circulation Biosystem in the University of Tsukuba, the Ciba-Geigy Foundation (Japan) for the Promotion of Science, the Asahi Glass Foundation, the Sumitomo Foundation, Ono Pharmaceutical Co., Ltd., and Sankyo Co., Ltd.

2Recipient of a fellowship from the Japanese Society for the Promotion of Science for Japanese Junior Scientists. Present address: Burnham Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA.


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