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(Received for publication, March 17, 1997, and in revised form, May 20, 1997)
From the Institute for Biochemistry II, University of
Göttingen, 37073 Göttingen, Germany
The two known mannose 6-phosphate receptors
(MPR46 and MPR300) both mediate the transport of Man-6-P-containing
lysosomal proteins to lysosomes. However, the MPRs cannot be detected
in lysosomes, instead they recycle between the plasma membrane and endosomes and between endosomes and the trans-Golgi network. Both, endocytosis from the plasma membrane and budding of transport vesicles
from the trans-Golgi network involves the interaction of the receptor
with the clathrin-coated vesicles-associated protein complexes AP1 and
AP2. We have analyzed this interaction between the Golgi-restricted AP1
complex and the plasma membrane-restricted AP2 complex with the MPR46
tail in vitro by using a biosensor.
AP1 and AP2 both bind to and dissociate from the MPR46 tail with
similar kinetics. Using synthetic peptides corresponding to different
MPR receptor tail regions in inhibition and binding studies, a common
high affinity binding site for AP1 and AP2 and two separate high
affinity binding sites for AP1 and AP2, respectively, were
identified.
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