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J. Biol. Chem., Vol. 278, Issue 6, 4063-4071, February 7, 2003
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From the Macropinocytosis is an efficient process for the
uptake of nutrients and solute macromolecules into cells from the
external environment. Macropinosomes, which are surrounded by actin,
are formed from the cell surface membrane ruffles and migrate toward the cell center. We have cloned the entire coding sequence of a member
of the Rab family small GTPases, Rah/Rab34. It lacked a consensus
sequence for GTP-binding/GTPase domain. Although wild-type Rah
exhibited extremely low GTPase activity in vitro, it
exerted appreciable GTPase activity in vivo. In
fibroblasts, Rah was colocalized with actin to the membrane ruffles and
membranes of relatively large vesicles adjacent to the ruffles. These
vesicles were identified as macropinosomes on the basis of several
criteria. Rah and Rab5 coexisted in some, but not all, macropinosomes.
Rah was predominantly associated with nascent macropinosomes, whereas
Rab5 was present in endosomes at later stages. The number of
macropinosomes in the cells overexpressing Rah increased about 2-fold.
The formation of macropinosomes by the treatment of platelet-derived
growth factor or phorbol ester was also facilitated by Rah but
suppressed by a dominant-negative Rah. Rah-promoted macropinosome
formation was retarded by dominant-negative mutants of Rac1 and WAVE2,
which are essential for membrane ruffling. These results imply that Rah
is required for efficient macropinosome formation from the membrane ruffles.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AB082927
Small GTPase Rah/Rab34 Is Associated with Membrane Ruffles and
Macropinosomes and Promotes Macropinosome Formation*
,,
,**
Department of Biology, Faculty of Science,
and Graduate School of Science and Technology, Chiba University,
Yayoicho, Inageku, Chiba 263-8522, the § Division of
Biochemistry and ¶ Division of Cancer Genomics, Institute of
Medical Science, University of Tokyo, Shirokanedai, Minatoku, Tokyo
108-8639, and ** CREST and PRESTO, Japan
Science and Technology Corporation, Kawaguchi, Saitama 332-0012, Japan
*
This work was supported by grants-in-aid from the Ministry
of Education, Culture, Sports, Science, and Technology of Japan and by
Research Grants (11B-1 and 14B-4) for Nervous and Mental Disorders from
the Ministry of Health, Labor, and Welfare of Japan.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Biology,
Faculty of Science, Chiba University, 1-33 Yayoicho, Inageku, Chiba
263-8522, Japan. Tel.: 81-43-290-3911; Fax: 81-43-290-3911; E-mail:
t.endo@faculty.chiba-u.jp.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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