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Vol. 11, Issue 12, 4227-4240, December 2000
and
*Division of Cell and Molecular Pathology, Department of Pathology,
University of Zürich, CH-8091 Zürich, Switzerland; and
Trimming of N-linked oligosaccharides by endoplasmic reticulum (ER)
glucosidase II is implicated in quality control of protein folding. An
alternate glucosidase II-independent deglucosylation pathway exists, in
which endo-Departments of Biological Chemistry and Medicine, Harvard
Medical School and the Joslin Diabetes Center, Boston, Massachusetts
02215
-mannosidase cleaves internally the glucose-substituted
mannose residue of oligosaccharides. By immunogold labeling, we
detected most endomannosidase in cis/medial Golgi
cisternae (83.8% of immunogold labeling) and less in the intermediate
compartment (15.1%), but none in the trans-Golgi apparatus and ER, including its transitional elements. This dual localization became more pronounced under 15°C conditions indicative of two endomannosidase locations. Under experimental conditions when
the intermediate compartment marker p58 was retained in peripheral sites, endomannosidase was redistributed to the Golgi apparatus. Double
immunogold labeling established a mutually exclusive distribution of
endomannosidase and glucosidase II, whereas calreticulin was observed
in endomannosidase-reactive sites (17.3% in intermediate compartment,
5.7% in Golgi apparatus) in addition to the ER (77%). Our results
demonstrate that glucose trimming of N-linked oligosaccharides is not
limited to the ER and that protein deglucosylation by endomannosidase in the Golgi apparatus and intermediate compartment additionally ensures that processing to mature oligosaccharides can continue. Thus,
endomannosidase localization suggests that a quality control of
N-glycosylation exists in the Golgi apparatus.
Corresponding author. E-mail address:
juergen.roth{at}pty.usz.ch.
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