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Volume 272, Number 29, Issue of July 18, 1997 pp. 18179-18184
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Ligand-induced Internalization of Cholecystokinin Receptors
DEMONSTRATION OF THE IMPORTANCE OF THE CARBOXYL TERMINUS FOR LIGAND-INDUCED INTERNALIZATION OF THE RAT CHOLECYSTOKININ TYPE B RECEPTOR BUT NOT THE TYPE A RECEPTOR

(Received for publication, January 22, 1997, and in revised form, May 13, 1997)

Markus Pohl Dagger , Sandrine Silvente-Poirot Dagger , Joseph R. Pisegna Dagger , Nadya I. Tarasova par and Stephen A. Wank Dagger

From the Dagger  Digestive Diseases Branch, NIDDK, National Institutes of Health, Bethesda, Maryland 20892 and par  Molecular Aspects of Drug Design Section, ABL-Basic Research Program, NCI-Frederick Cancer Research and Development Center, Frederick, Maryland 21702

Internalization of a variety of different heptahelical G protein-coupled receptors has been shown to be influenced by a number of different structural determinants of the receptors, including the carboxyl terminus. To investigate the role of the carboxyl terminus of cholecystokinin (CCK) receptors in receptor internalization, the rat wild type (WT) CCK-A receptor (WT CCKAR) and the rat WT CCK-B receptor (WT CCKBR) were truncated after amino acid residue 399 (CCKAR Tr399) and 408 (CCKBR Tr408), thereby deleting the carboxyl-terminal 45 and 44 residues, respectively. All WT and mutant CCK receptors were stably expressed in NIH/3T3 cells. Internalization of the CCKAR Tr399 was not significantly different from the WT CCKAR. In contrast, internalization of the CCKBR Tr408 was decreased to 26% compared with the WT CCKBR internalization of 92%. The mutation of all 10 serine and threonine residues (as potential phosphorylation sites) in the carboxyl terminus of the CCKBR to alanines (mutant CCKBR Delta S/T) could account for the majority of this effect (39% internalization). All mutant receptors displayed similar ligand binding characteristics, G protein coupling, and signal transduction as their respective WT receptors, indicating that the carboxyl termini are not necessary for these processes. Thus, internalization of the CCKBR, unlike that of the CCKAR, depends on the carboxyl terminus of the receptor. These results suggest that, despite the high degree of homology between CCKAR and CCKBR, the structural determinants that mediate the interaction with the endocytic pathway reside in different regions of the receptors.


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