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J Biol Chem, Vol. 274, Issue 26, 18524-18535, June 25, 1999
From the Departments of Proteases cleave proteinase-activated receptors
(PARs) to expose N-terminal tethered ligands that bind and activate the
cleaved receptors. The tethered ligand, once exposed, is always
available to interact with its binding site. Thus, efficient mechanisms must prevent continuous activation, including receptor phosphorylation and uncoupling from G-proteins, receptor endocytosis, and lysosomal degradation.
Trafficking of Proteinase-activated Receptor-2 and
-Arrestin-1
Tagged with Green Fluorescent Protein
-ARRESTIN-DEPENDENT ENDOCYTOSIS OF A PROTEINASE RECEPTOR
,,, and¶
Surgery and
¶ Physiology, University of California,
San Francisco, California 94143-0660 and § CURE
Digestive Diseases Research Center, West Los Angeles Veterans Affairs
Medical Center, and Department of Medicine, UCLA Medical School,
Los Angeles, California 90073-1792
-Arrestins mediate uncoupling and endocytosis of certain neurotransmitter receptors, which are activated in a reversible manner. However, the role of -arrestins in trafficking of PARs, which are irreversibly activated, and the effects of proteases on the
subcellular distribution of -arrestins have not been examined. We
studied trafficking of PAR2 and -arrestin1 coupled to green fluorescent protein. Trypsin induced the following: (a)
redistribution of -arrestin1 from the cytosol to the plasma
membrane, where it co-localized with PAR2; (b)
internalization of -arrestin1 and PAR2 into the same early
endosomes; (c) redistribution of -arrestin1 to the
cytosol concurrent with PAR2 translocation to lysosomes; and
(d) mobilization of PAR2 from the Golgi apparatus to the
plasma membrane. Overexpression of a C-terminal fragment of
-arrestin-319-418, which interacts constitutively with
clathrin but does not bind receptors, inhibited agonist-induced
endocytosis of PAR2. Our results show that -arrestins mediate
endocytosis of PAR2 and support a role for -arrestins in uncoupling
of PARs.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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