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Cited by 175Protein Kinase Regulation and GTPase SignalingCellular transport and secretionMicrotubule and mitosis dynamics

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The identification and characterization of a GDP-dissociation inhibitor (GDI) for the CDC42Hs protein

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Leonard, D, Hart, M.J., Platko, J.V., Eva, A, Henzel, W, Evans, T, Cerione, R.A.·1992·Journal of Biological Chemistry
DOI 10.1016/s0021-9258(18)50026-0
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Abstract

The ras-related protein, CDC42Hs, is a 22-kDa GTP-binding protein which is the human homolog of a Saccharomyces cerevisiae yeast-cell-division cycle protein. In attempting to isolate and biochemically characterize mammalian proteins capable of regulating various activities of CDC42Hs, we have identified an activity in bovine brain cytosol which effectively inhibits the dissociation of [3H]GDP from the platelet- or the Spodoptera frugiperda-expressed CDC42Hs protein. The purification of this activity was achieved by a series of steps which included ammonium sulfate fractionation, DEAE-Sephacel, Mono-Q, and Mono-S chromatographies. The purified CDC42Hs regulatory protein has an apparent molecular weight of 28,000, and cyanogen bromide-generated peptide sequences of this protein were identical to sequences from the carboxyl-terminal portion of rho-GDP-dissociation inhibitor (rho-GDI) (Fukumoto, Y., Kaibuchi, K., Hori, Y., Fujioka, H., Araki, S., Ueda, T., Kikuchi, A., and Takai, Y. (1990) Oncogene 5, 1321-1328). In addition, an Escherichia coli-expressed, glutathione S-transferase-rho-GDI fusion protein fully substitutes for the GDI which we have purified from bovine brain in its ability to inhibit GDP dissociation from CDC42Hs. These findings suggest either that a common regulatory protein (GDI) is capable of inhibiting GDP dissociation from the rho and CDC42Hs proteins or that these two GTP-binding proteins interact with GDI proteins of very similar structure. The purified bra…

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Metadata

Authors
Leonard, D., Hart, M. J., Platko, J. V., Eva, A., Henzel, W., Evans, T., & Cerione, R. A.
Affiliations
  • Cornell University (US)
  • National Institutes of Health (US)
  • Genentech (US)
ORCID
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1992-11
Volume
267
Issue
32
Pages
22860-22868
ISSN
0021-9258 (ISSN-L)
DOI
10.1016/s0021-9258(18)50026-0
OpenAlex
W2126542941
Cited by
175
References
0
Citations by year
2025: 1 · 2024: 3 · 2023: 1 · 2022: 3 · 2021: 2 · 2020: 4 · 2019: 3 · 2017: 3 · 2016: 1 · 2015: 3 · 2014: 6 · 2013: 3 · 2012: 10
FWCI
3.81
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Funders
National Institute of General Medical Sciences (GM 47458, R01GM047458)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
Keywords
2H, GDP dissociation inhibitor, RhoGDI, G proteins, brain cytosol, guanine nucleotide exchange, protein purification, GST fusion protein, protein-protein interaction
MeSH terms
Amino Acid Sequence, Animals, Blood Platelets, Brain, Cattle, Cell Line, Cell Membrane, Chromatography, Ion Exchange, Cloning, Molecular, Cytosol, Escherichia coli, Guanosine Diphosphate, Humans, Kinetics, Molecular Sequence Data, Moths, Recombinant Proteins, Transfection, Sequence Homology, Amino Acid, GTP-Binding Proteins, Guanine Nucleotide Dissociation Inhibitors, cdc42 GTP-Binding Protein, rho-Specific Guanine Nucleotide Dissociation Inhibitors

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