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J. Biol. Chem., Vol. 275, Issue 22, 16827-16836, June 2, 2000
From the A novel, retinoic acid-induced gene,
GRP1-associated scaffold
protein (GRASP), was isolated from P19 embryonal carcinoma
cells using a subtractive screening strategy. GRASP was found to be highly expressed in brain and exhibited lower levels of expression in
lung, heart, embryo, kidney, and ovary. The predicted amino acid
sequence of GRASP is characterized by several putative protein-protein interaction motifs, suggesting that GRASP may be a component of a
larger protein complex in the cell. Although GRASP does not harbor a
predicted membrane spanning domain(s), the protein was observed to be
associated with the plasma membrane of transiently transfected
mammalian cells. Yeast two-hybrid screening revealed that GRASP
interacted strongly with the General Receptor
for Phosphoinositides 1 (GRP1), a brefeldin
A-insensitive guanine nucleotide exchange factor for the
ADP-ribosylation factor family of proteins. GRASP·GRP1 interactions
were also demonstrated in vitro and in mammalian cells in
which GRASP was shown to enhance GRP1 association with the plasma
membrane. Furthermore, GRASP colocalized with endogenous ADP-ribosylation factors at the plasma membrane in transfected cells,
suggesting that GRASP may modulate signaling by this family of small GTPases.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF236099.
Interaction of GRASP, a Protein encoded by a Novel Retinoic
Acid-induced Gene, with Members of the Cytohesin Family of Guanine
Nucleotide Exchange Factors*
§¶,
**,,§§§,,§
Programs in Molecular and Cellular Biology
and Toxicology, § Laboratory of Molecular Pharmacology,
College of Pharmacy, Environmental Health Sciences Center, and
Department of Microbiology, Oregon State
University, Corvallis, Oregon 97331 and the ¶¶ Molecular
Medicine Research Institute, Mountain View, California 94043
*
This work was supported in part by Grant CA51993 from the
NCI, National Institutes of Health (to M. I. D. and M. L.).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.
Established Investigator of the American Heart
Association (AHA); supported by AHA Grant 9640219N. To whom
correspondence should be addressed: Laboratory of Molecular
Pharmacology, College of Pharmacy, Oregon State University, Corvallis,
OR 97331. Tel.: 541-737-5809; Fax: 541-737-3999; E-mail:
mark.leid@orst.edu.
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