Molecular characterization of a novel RhoGAP, RRC-1 of the nematode Caenorhabditis elegans

Journal Article · Fri Jun 01 00:00:00 EDT 2007 · Biochemical and Biophysical Research Communications

DOI:https://doi.org/10.1016/j.bbrc.2007.03.192· OSTI ID:20991364

Delawary, Mina ^[1]; Nakazawa, Takanobu ^[1]; Tezuka, Tohru ^[1]; Sawa, Mariko ^[2]; Iino, Yuichi ^[3]; Takenawa, Tadaomi ^[2]; Yamamoto, Tadashi ^[1]

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1. Division of Oncology, Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639 (Japan)
2. Division of Biochemistry, Institute of Medical Science, University of Tokyo (Japan)
3. Molecular Genetics Research Laboratory, Graduate School of Science, University of Tokyo (Japan)

The GTPase-activating proteins for Rho family GTPases (RhoGAP) transduce diverse intracellular signals by negatively regulating Rho family GTPase-mediated pathways. In this study, we have cloned and characterized a novel RhoGAP for Rac1 and Cdc42, termed RRC-1, from Caenorhabditis elegans. RRC-1 was highly homologous to mammalian p250GAP and promoted GTP hydrolysis of Rac1 and Cdc42 in cells. The rrc-1 mRNA was expressed in all life stages. Using an RRC-1::GFP fusion protein, we found that RRC-1 was localized to the coelomocytes, excretory cell, GLR cells, and uterine-seam cell in adult worms. These data contribute toward understanding the roles of Rho family GTPases in C. elegans.

• OSTI ID: 20991364
• Journal Information: Biochemical and Biophysical Research Communications, Vol. 357, Issue 2; Other Information: DOI: 10.1016/j.bbrc.2007.03.192; PII: S0006-291X(07)00623-7; Copyright (c) 2007 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
• Country of Publication: United States
• Language: English

Related Subjects

60 APPLIED LIFE SCIENCES
HYDROLYSIS
MOLECULAR BIOLOGY
MOLECULAR STRUCTURE
NEMATODES
PROTEINS