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J Biol Chem, Vol. 273, Issue 21, 12967-12972, May 22, 1998
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From the To understand what processes contribute to the
agonist-induced internalization of subtypes of muscarinic acetylcholine
receptors, we analyzed the role of arrestins. Whereas the m2 mAChR has
been shown to undergo augmented internalization when arrestins 2 and 3 are overexpressed (Pals-Rylaarsdam, R., Gurevich, V. V., Lee, K. B., Ptasienski, J. A., Benovic, J. L., and Hosey,
M. M. (1997) J. Biol. Chem. 272, 23682-23689),
the agonist-induced internalization of m1, m3, and m4 mAChRs was
unchanged when arrestins 2 or 3 were overexpressed in transiently
transfected HEK-tsA201 cells. Furthermore, when a dominant-negative
arrestin was used to interrupt endogenous arrestin function, there was
no change in the internalization of the m1, m3, and m4 mAChR whereas
the internalization of the Department of Molecular Pharmacology and
Biological Chemistry and the ¶ Institute of Neuroscience,
Northwestern University Medical School, Chicago, Illinois 60611 and the
** Department of Microbiology and Immunology, Kimmel Cancer Institute,
Thomas Jefferson University, Philadelphia, Pennsylvania 19107
2 adrenergic receptor was
completely blocked. Wild-type and GTPase-deficient dominant-negative
dynamin were used to determine which endocytic machinery played a role
in the endocytosis of the subtypes of mAChRs. Interestingly, when
dynamin function was blocked by overexpression of the GTPase-deficient
dynamin, agonist- induced internalization of the the m1, m3, and m4
mAChRs was suppressed. These results suggested that the internalization
of the m1, m3, and m4 mAChRs occurs via an arrestin-independent but
dynamin-dependent pathway. To ascertain whether domains
that confer arrestin sensitivity and dynamin insensitivity could be
functionally exchanged between subtypes of mAChRs, chimeric m2/m3
receptors were analyzed for their properties of agonist-induced
internalization. The results demonstrated that the third intracellular
loop of the m2 mAChR conferred arrestin sensitivity and dynamin
insensitivity to the arrestin-insensitive, dynamin-sensitive m3 mAChR
while the analogous domain of the m3 mAChR conferred arrestin
resistance and dynamin sensitivity to the previously
arrestin-sensitive, dynamin-insensitive m2 mAChR.
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