Polarized apical targeting directed by the signal/anchor region of simian virus 5 hemagglutinin-neuraminidase

Xue F. Huang, Richard W. Compans, Siyi Chen, Robert A. Lamb, Peter Arvan*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

25 Scopus citations


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 clearable 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.

Original languageEnglish (US)
Pages (from-to)27598-27604
Number of pages7
JournalJournal of Biological Chemistry
Issue number44
StatePublished - Oct 31 1997

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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