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J Biol Chem, Vol. 274, Issue 38, 26860-26868, September 17, 1999
From the Institut für Medizinische Mikrobiologie,
Medizinische Hochschule Hannover, Carl-Neuberg-Straße 1, D-30625 Hannover, Germany
The leukocyte response to chemoattractants is
transduced by the interaction of transmembrane receptors with
GTP-binding regulatory proteins (G-proteins). RGS1 is a member of a
protein family constituting a newly appreciated and large group of
proteins that act as deactivators of G-protein signaling pathways by
accelerating the GTPase activity of G-protein 
subunits. We
demonstrate here that RGS1 is expressed in human monocytes; by
immunofluorescence and subcellular fractionation RGS1 was localized to
the plasma membrane. By using a mixture of RGS1 and plasma membranes,
we were able to demonstrate GAP activity of RGS1 on receptor-activated
G-proteins; RGS1 did not affect ligand-stimulated GDP-GTP exchange. We
found that RGS1 desensitizes a variety of chemotactic receptors
including receptors for
N-formyl-methionyl-leucyl-phenylalanine, leukotriene B4,
and C5a. Interaction of RGS proteins and ligand-induced G-protein signaling can be demonstrated by determining GTPase activity using purified RGS proteins and plasma membranes.
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