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3 results on '"Koling S"'

1. ADP-ribosylation factor (ARF)-like 4, 6, and 7 represent a subgroup of the ARF family characterization by rapid nucleotide exchange and a nuclear localization signal.

Author

Jacobs S, Schilf C, Fliegert F, Koling S, Weber Y, Schürmann A, and Joost HG

Subjects
ADP-Ribosylation Factor 1, ADP-Ribosylation Factors, Amino Acid Sequence, Animals, COS Cells metabolism, Cloning, Molecular, Esophagus chemistry, Female, GTP Phosphohydrolases genetics, Green Fluorescent Proteins, Humans, Kidney chemistry, Luminescent Proteins genetics, Luminescent Proteins metabolism, Male, Molecular Sequence Data, RNA, Messenger analysis, Recombinant Proteins genetics, Recombinant Proteins metabolism, Sequence Analysis, Sequence Homology, Amino Acid, Subcellular Fractions, Testis chemistry, Transfection, Uterus chemistry, Cell Nucleus metabolism, GTP Phosphohydrolases metabolism, GTP-Binding Proteins genetics, GTP-Binding Proteins metabolism, Guanine metabolism
Abstract

The novel ARF-like GTPase ARL7 is a close relative of ARL4 and ARL6 (71% and 59%) identical amino acids). A striking characteristic of these GTPases is their basic C-terminus which, when fused to the C-terminus of green fluorescent protein (GFP), targets the constructs to the nucleus of transfected COS-7 cells. Full length ARL4 was detected in both nuclear and extranuclear compartments, whereas a construct of ARL4 lacking its C-terminus was excluded from the nucleus. Nucleotide exchange rates of recombinant ARL4, ARL6 and ARL7 were similar and appeared considerably higher than those of other members of the ARF family (ARF1, ARP). It is concluded that ARL4, ARL6 and ARL7 form a subgroup within the ARF family with similar, possibly nuclear, function.

Published
1999
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2. The ADP-ribosylation factor (ARF)-related GTPase ARF-related protein binds to the ARF-specific guanine nucleotide exchange factor cytohesin and inhibits the ARF-dependent activation of phospholipase D.

Author

Schürmann A, Schmidt M, Asmus M, Bayer S, Fliegert F, Koling S, Massmann S, Schilf C, Subauste MC, Voss M, Jakobs KH, and Joost HG

Subjects
ADP-Ribosylation Factors, Carbachol metabolism, Cell Line, Enzyme Activation, Guanosine Triphosphate metabolism, Humans, Receptor, Muscarinic M3, Receptors, Muscarinic metabolism, Signal Transduction, Yeasts, Cell Adhesion Molecules metabolism, GTP Phosphohydrolases metabolism, GTP-Binding Proteins metabolism, GTPase-Activating Proteins, Guanine Nucleotide Exchange Factors, Membrane Proteins metabolism, Phospholipase D metabolism, Proteins metabolism, Sequence Homology, Amino Acid
Abstract

ADP-ribosylation factor-related protein (ARP) is a membrane-associated GTPase with remote similarity to the family of ADP-ribosylation factors (ARF). In a yeast two-hybrid screen designed to identify proteins interacting with ARP, we isolated a partial cDNA of the ARF-specific guanine nucleotide exchange factor mSec7-1/cytohesin encoding its N terminus and most of the Sec7 domain (codons 1-200). ARP and ARP-Q79L (GTPase-negative ARP) exhibited a higher affinity to mSec7-1-(1-200) than ARP-T31N (nucleotide exchange-defective ARP) in the two-hybrid assay. Similarly, full-length [35S]mSec7-1/cytohesin was specifically adsorbed to glutathione-Sepharose loaded with glutathione S-transferase (GST)-ARP-Q79L, GST-ARP, or GST-ARP-T31N, the latter exhibiting the lowest binding affinity. Overexpression of ARP-Q79L, but not of ARP-T31N, in COS-7 cells reduced the fluorescence from co-expressed green fluorescent protein fused with mSec7-1/cytohesin or mSec7-2/ARNO in plasma membranes as detected by deconvolution microscopy. Recombinant ARP and ARP-Q79L, but not ARP-T31N, inhibited the phospholipase D (PLD) activity stimulated by mSec7-2/ARNO and ARF in a system of isolated membranes. Furthermore, transfection of HEK-293 cells with ARP or ARP-Q79L, but not ARP-T31N, inhibited the muscarinic acetylcholine receptor-3 induced PLD stimulation and translocation of ARF from cytosol to membranes. These data suggest that the GTP-bound form of ARP specifically binds mSec7-1/cytohesin, and that ARP may be involved in a pathway inhibiting the ARF-controlled activity of PLD.

Published
1999
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3. The ADP-ribosylation factor (ARF)-related GTPase ARF-related protein binds to the ARF-specific guanine nucleotide exchange factor cytohesin and inhibits the ARF-dependent activation of phospholipase D

Author

HG Joost, Karl Jakobs, Subauste Mc, Koling S, Massmann S, Bayer S, Martina Schmidt, Matthias Voss, Asmus M, Annette Schürmann, Schilf C, and Fliegert F

Subjects
ADP ribosylation factor, GTPase-activating protein, GTPase, Guanosine triphosphate, Biology, Biochemistry, Cell Line, GTP Phosphohydrolases, chemistry.chemical_compound, Enzyme activator, GTP-binding protein regulators, GTP-Binding Proteins, Yeasts, Phospholipase D, Guanine Nucleotide Exchange Factors, Humans, Molecular Biology, Receptor, Muscarinic M3, Sequence Homology, Amino Acid, ADP-Ribosylation Factors, GTPase-Activating Proteins, Membrane Proteins, Proteins, Cell Biology, Molecular biology, Receptors, Muscarinic, Cell biology, Enzyme Activation, chemistry, Carbachol, Guanine nucleotide exchange factor, Guanosine Triphosphate, Cell Adhesion Molecules, Signal Transduction
Abstract

ADP-ribosylation factor-related protein (ARP) is a membrane-associated GTPase with remote similarity to the family of ADP-ribosylation factors (ARF). In a yeast two-hybrid screen designed to identify proteins interacting with ARP, we isolated a partial cDNA of the ARF-specific guanine nucleotide exchange factor mSec7-1/cytohesin encoding its N terminus and most of the Sec7 domain (codons 1-200). ARP and ARP-Q79L (GTPase-negative ARP) exhibited a higher affinity to mSec7-1-(1-200) than ARP-T31N (nucleotide exchange-defective ARP) in the two-hybrid assay. Similarly, full-length [35S]mSec7-1/cytohesin was specifically adsorbed to glutathione-Sepharose loaded with glutathione S-transferase (GST)-ARP-Q79L, GST-ARP, or GST-ARP-T31N, the latter exhibiting the lowest binding affinity. Overexpression of ARP-Q79L, but not of ARP-T31N, in COS-7 cells reduced the fluorescence from co-expressed green fluorescent protein fused with mSec7-1/cytohesin or mSec7-2/ARNO in plasma membranes as detected by deconvolution microscopy. Recombinant ARP and ARP-Q79L, but not ARP-T31N, inhibited the phospholipase D (PLD) activity stimulated by mSec7-2/ARNO and ARF in a system of isolated membranes. Furthermore, transfection of HEK-293 cells with ARP or ARP-Q79L, but not ARP-T31N, inhibited the muscarinic acetylcholine receptor-3 induced PLD stimulation and translocation of ARF from cytosol to membranes. These data suggest that the GTP-bound form of ARP specifically binds mSec7-1/cytohesin, and that ARP may be involved in a pathway inhibiting the ARF-controlled activity of PLD.

Published
1999

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