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J. Biol. Chem., Vol. 276, Issue 49, 46597-46604, December 7, 2001
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From the Department of Physiological Chemistry, School of
Veterinary Medicine Hanover, Bünteweg 17, Hanover D-30559,
Germany
The apical sorting of the small intestinal
membrane glycoprotein sucrase-isomaltase (SI) depends on the presence
of O-linked glycans and the transmembrane domain. Here, we
investigate the role of O-glycans carried by the
Ser/Thr-rich stalk region of SI as an apical sorting signal and
evaluate the spatial requirements for an efficient recognition of this
signal. Several hybrid proteins are generated comprising the unsorted
and unglycosylated protein, the rat growth hormone (rGH), fused to
either the transmembrane domain of SI (GH-SITM), or the
transmembrane and the stalk domains (GH-SISR/TM). Both
constructs are randomly distributed over the apical and basolateral
membranes of MDCK cells indicating that neither the transmembrane
domain nor the O-glycans are sufficient per se
for an apical delivery. Only when a polyglycine spacer is inserted
between the stalk region of SI and the luminal part of rGH in the
GH-SIGly/SR/TM fusion protein does efficient apical sorting
of an O-glycosylated protein as well as a
time-dependent association with detergent-insoluble lipid
microdomains occur. Obviously, the polyglycine spacer facilitates the
accessibility of the O-glycans in
GH-SIGly/SR/TM to a putative sorting receptor, whereas
these glycans are inadequately recognized in GH-SISR/TM. We
conclude that the O-glycans in the stalk region of SI act
as an apical sorting signal within a sorting machinery that comprises at least a carbohydrate-binding protein and fulfills specific spatial
requirements provided, for example by a polyglycine spacer in the
context of rGH or the P-domain within the SI enzyme complex.
Characteristics and Structural Requirements of Apical Sorting of
the Rat Growth Hormone through the O-Glycosylated Stalk
Region of Intestinal Sucrase-isomaltase*
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Tel.: 49-511-953-8780;
Fax: 49-511-953-8585; E-mail: hassan.naim@tiho-hannover.de.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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