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(Received for publication, July 22, 1997, and in revised form, August 28, 1997)
From the To examine the possibility of independent
cytoplasmic/transmembrane domain-based apical sorting, we have
investigated paramyxovirus SV5 hemagglutinin-neuraminidase (HN), a type
II membrane protein with a small N-terminal signal/anchor region. In
SV5-infected Madin-Darby canine kidney (MDCK) cells, >90% of HN is
found on the apical surface. We have expressed chimeric proteins in
which the N terminus of HN, including its signal/anchor region, is
attached to a (normally cytosolic) reporter pyruvate kinase (PK). PK
itself expressed immediately downstream from a cleavable signal peptide was converted to a 58-kDa N-linked glycosylated form, which
was secreted predominantly (80%) to the basolateral surface of MDCK cells. By contrast, stably expressed PK chimeras, now anchored as type
II membrane proteins with either the first 48 or 72 amino acids of HN,
received similar N-linked glycosylation, yet exhibited polarized transport with a preferentially (75%) apical distribution. These results suggest that the N-terminal signal/anchor region of HN
contains independent sorting information for apical specific targeting
in MDCK cells.
Volume 272, Number 44,
Issue of October 31, 1997
pp. 27598-27604
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
Polarized Apical Targeting Directed by the Signal/Anchor
Region of Simian Virus 5 Hemagglutinin-Neuraminidase
,
and
Department of Microbiology, University of
Alabama at Birmingham, Birmingham, Alabama 35209, the
§ Department of Microbiology and Immunology, Emory
University School of Medicine, Atlanta, Georgia 30322, the
¶ Department of Cancer Biology, Comprehensive Cancer Center,
Bowman Gray School of Medicine, Wake Forest University, Winston-Salem,
North Carolina 27157, the 
Howard Hughes Medical Institute and
Department of Biochemistry, Molecular Biology, and Cell Biology,
Northwestern University, Evanston, Illinois 60208-3500, and the
Division of Endocrinology and Department of
Developmental and Molecular Biology, Albert Einstein College of
Medicine, Bronx, New York 10461
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