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(Received for publication, June 14, 1996, and in revised form, October 24, 1996)
From the Department of Physiology, School of Medicine, and
Molecular Biology Institute, University of California,
Los Angeles, California 90095-1751
We have characterized the maturation of Shaker
K+ channel protein and the cellular site of assembly of
pore-forming
Volume 272, Number 5,
Issue of January 31, 1997
pp. 3022-3027
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
and 
Subunits Assemble in the
Endoplasmic Reticulum
and cytoplasmic 
subunits in a transfected
mammalian cell line. Shaker protein is made as a partially
glycosylated, immature precursor that is converted to a fully
glycosylated, mature product. Shaker protein did not mature when
transport from the endoplasmic reticulum (ER) to the Golgi apparatus
was blocked. Consistent with this finding, only the immature form was
sensitive to digestion with endoglycosidase H. These results indicate
that the immature protein is core-glycosylated in the ER, whereas the
oligosaccharides of the mature protein have been further processed in
the Golgi compartment. After inhibiting ER-to-Golgi transport, the
oligomeric state of Shaker subunits was assessed by cross-linking in
intact cells or by solubilization and sucrose gradient sedimentation.
The results indicate that Shaker subunits assemble with each other in
the ER. When co-expressed, the Kv2 subunit also associated with
Shaker in the ER. Assembly with the 2 subunit did not increase the
rate or extent of Shaker protein maturation. Our results indicate that
the biogenesis of Shaker K+ channels in vivo
involves core glycosylation and subunit assembly in the ER, followed by
efficient transfer to the Golgi apparatus where the oligosaccharides
are modified.
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