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J. Biol. Chem., Vol. 277, Issue 21, 19008-19018, May 24, 2002
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From The Institute for Enzyme Research, The University of
Tokushima, 3-18-15 Kuramoto, Tokushima 770-8503, Japan and
¶ Department of Biochemistry, Faculty of Medicine, Hiroshima
University, 1-2-3 Kasumi, Minami-ku, Hiroshima 734-8551, Japan
Using yeast two-hybrid screening, we
have identified a mouse Postsynaptic density 95/Discs large/Zona
occludens-1 (PDZ) protein that interacts with activin type II receptors
(ActRIIs). We named the protein activin receptor-interacting protein 2 (ARIP2). ARIP2 was found to have one PDZ domain in the
NH2-terminal region and interact specifically with
ActRIIs among the receptors for the transforming growth factor The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AF414433.
Regulation of Endocytosis of Activin Type II Receptors
by a Novel PDZ Protein through Ral/Ral-binding Protein
1-dependent Pathway*
,
, and
family by the PDZ domain. Interestingly, overexpression of ARIP2
enhances endocytosis of ActRIIs and reduces activin-induced
transcription in Chinese hamster ovary K1 cells. In addition,
immunofluorescence co-localization studies indicated the direct
involvement of ARIP2 in the intracellular translocation of ActRIIs by
PDZ domain-mediated interaction. Moreover, we have identified that the
COOH-terminal region of ARIP2 interacts with Ral-binding protein 1 (RalBP1). RalBP1 is a potential effector protein of small GTP-binding
protein Ral and regulates endocytosis of epidermal growth factor and
insulin receptors. The studies using deletion mutants of RalBP1 and
constitutively GTP and GDP binding forms of Ral indicate that ARIP2
regulates endocytosis of ActRIIs through the
Ral/RalBP1-dependent pathway, and the GDP-GTP exchange of
Ral is critical for this regulation.
*
This research was supported by the Ministry of Education,
Science, Sports, Culture, and Technology of Japan and also by grants from The Inamori Foundation for Research and Kyowa Hakko Kogyo Co.,
Ltd.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.
Present address: Dept. of Animal Reproduction, National Institute
of Animal Industry, Ministry of Agriculture, Forestry and Fisheries,
Tsukuba, Ibaraki 305-0991, Japan.
§
Present address: Dept. of Immunology, School of Basic Medical
Sciences, University of Jilin, 2 Xinmin St., Changchun 130021, People's Republic of China.
To whom correspondence should be addressed. Tel.:
81-88-633-7439; Fax: 81-88-633-7440; E-mail:
tsuchida@ier.tokushima-u.ac.jp.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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