Topology of eukaryotic type II membrane proteins: Importance of N-terminal positively charged residues flanking the hydrophobic domain

Griffith D. Parks*, Robert A. Lamb

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

123 Scopus citations

Abstract

We have tested the role of different charged residues flanking the sides of the signal/anchor (S/A) domain of a eukaryotic type II (NcytCexo) integral membrane protein in determining its topology. The removal of positively charged residues on the N-terminal side of the S/A yields proteins with an inverted topology, while the addition of positively charged residues to only the C-terminal side has very little effect on orientation. Expression of chimeric proteins composed of domains from a type II protein (HN) and the oppositely oriented membrane protein M2 indicates that the HN N-terminal domain is sufficient to confer a type II topology and that the M2 N-terminal ectodomain can direct a type II topology when modified by adding positively charged residues. These data suggest that eukaryotic membrane protein topology is governed by the presence or absence of an N-terminal signal for retention in the cytoplasm that is composed in part of positive charges.

Original languageEnglish (US)
Pages (from-to)777-787
Number of pages11
JournalCell
Volume64
Issue number4
DOIs
StatePublished - Feb 22 1991

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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