PMID- 10092663
OWN - NLM
STAT- MEDLINE
DCOM- 19990427
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 14
DP  - 1999 Apr 2
TI  - 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.
PG  - 9744-51
AB  - 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.
FAU - Schurmann, A
AU  - Schurmann A
AD  - Institut fur Pharmakologie und Toxikologie, Medizinische Fakultat der
      Rheinisch-Westfalischen Technischen Hochschule Aachen, D-52074 Aachen, Germany.
FAU - Schmidt, M
AU  - Schmidt M
FAU - Asmus, M
AU  - Asmus M
FAU - Bayer, S
AU  - Bayer S
FAU - Fliegert, F
AU  - Fliegert F
FAU - Koling, S
AU  - Koling S
FAU - Massmann, S
AU  - Massmann S
FAU - Schilf, C
AU  - Schilf C
FAU - Subauste, M C
AU  - Subauste MC
FAU - Voss, M
AU  - Voss M
FAU - Jakobs, K H
AU  - Jakobs KH
FAU - Joost, H G
AU  - Joost HG
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (GTPase-Activating Proteins)
RN  - 0 (Guanine Nucleotide Exchange Factors)
RN  - 0 (Membrane Proteins)
RN  - 0 (Proteins)
RN  - 0 (Receptor, Muscarinic M3)
RN  - 0 (Receptors, Muscarinic)
RN  - 0 (Sec7 guanine nucleotide exchange factors)
RN  - 0 (cytohesin-1)
RN  - 0 (cytohesin-2)
RN  - 86-01-1 (Guanosine Triphosphate)
RN  - 8Y164V895Y (Carbachol)
RN  - EC 3.1.4.4 (Phospholipase D)
RN  - EC 3.6.1.- (ADP-ribosylation factor related proteins)
RN  - EC 3.6.1.- (GTP Phosphohydrolases)
RN  - EC 3.6.1.- (GTP-Binding Proteins)
RN  - EC 3.6.5.2 (ADP-Ribosylation Factors)
SB  - IM
MH  - ADP-Ribosylation Factors
MH  - Carbachol/metabolism
MH  - Cell Adhesion Molecules/*metabolism
MH  - Cell Line
MH  - Enzyme Activation
MH  - GTP Phosphohydrolases/*metabolism
MH  - GTP-Binding Proteins/*metabolism
MH  - *GTPase-Activating Proteins
MH  - *Guanine Nucleotide Exchange Factors
MH  - Guanosine Triphosphate/metabolism
MH  - Humans
MH  - Membrane Proteins/*metabolism
MH  - Phospholipase D/*metabolism
MH  - Proteins/*metabolism
MH  - Receptor, Muscarinic M3
MH  - Receptors, Muscarinic/metabolism
MH  - *Sequence Homology, Amino Acid
MH  - Signal Transduction
MH  - Yeasts
EDAT- 1999/03/27 00:00
MHDA- 1999/03/27 00:01
CRDT- 1999/03/27 00:00
PHST- 1999/03/27 00:00 [pubmed]
PHST- 1999/03/27 00:01 [medline]
PHST- 1999/03/27 00:00 [entrez]
AID - 10.1074/jbc.274.14.9744 [doi]
AID - S0021-9258(19)87312-X [pii]
PST - ppublish
SO  - J Biol Chem. 1999 Apr 2;274(14):9744-51. doi: 10.1074/jbc.274.14.9744.