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J. Cell Biol.,
Volume 143, Number 4, November 16, 1998 1041-1052
-Tubulin
* Department of Molecular Biology, A novel human protein with a molecular
mass of 55 kD, designated RanBPM, was isolated with
the two-hybrid method using Ran as a bait. Mouse and
hamster RanBPM possessed a polypeptide identical to
the human one. Furthermore, Saccharomyces cerevisiae
was found to have a gene, YGL227w, the COOH-terminal half of which is 30% identical to RanBPM. Anti-RanBPM antibodies revealed that RanBPM was localized within the centrosome throughout the cell cycle. Overexpression of RanBPM produced multiple spots
which were colocalized with Department of Surgery, and ¶ Department of Neurosurgery, Graduate School of Medical
Science, Kyushu University, Fukuoka 812-82, Japan; § Laboratory of Cellular and Molecular Biology, The Institute of Physical
and Chemical Research (RIKEN) 2-1 Hirosawa, Wako, Saitama 351-01, Japan; ** Inheritance and Variation Group,
PRESTO, Japan Science and Technology Corporation, Kyoto 619-0237, Japan; and Department of Biophysics, Faculty of
Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan
-tubulin and acted as
ectopic microtubule nucleation sites, resulting in a reorganization of microtubule network. RanBPM cosedimented with the centrosomal fractions by sucrose-
density gradient centrifugation. The formation of
microtubule asters was inhibited not only by anti-
RanBPM antibodies, but also by nonhydrolyzable
GTP-Ran. Indeed, RanBPM specifically interacted
with GTP-Ran in two-hybrid assay. The central part of
asters stained by anti-RanBPM antibodies or by the
mAb to -tubulin was faded by the addition of GTPS-Ran, but not by the addition of anti-RanBPM anti-
bodies. These results provide evidence that the Ran-binding protein, RanBPM, is involved in microtubule
nucleation, thereby suggesting that Ran regulates the
centrosome through RanBPM.
-tubulin;
Ran;
RanBPM;
YGL227w
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