Bipartite signals mediate subcellular targeting of tail-anchored membrane proteins in Saccharomyces cerevisiae

J Biol Chem. 2003 Mar 7;278(10):8219-23. doi: 10.1074/jbc.M212725200. Epub 2003 Jan 3.

Abstract

Tail-anchored proteins have an NH(2)-terminal cytosolic domain anchored to intracellular membranes by a single, COOH-terminal, transmembrane segment. Sequence analysis identified 55 tail-anchored proteins in Saccharomyces cerevisiae, with several novel proteins, including Prm3, which we find is required for karyogamy and is tail-anchored in the nuclear envelope. A total of six tail-anchored proteins are present in the mitochondrial outer membrane and have relatively hydrophilic transmembrane segments that serve as targeting signals. The rest, by far the majority, localize via a bipartite system of signals: uniformly hydrophobic tail anchors are first inserted into the endoplasmic reticulum, and additional segments within the cytosolic domain of each protein can dictate subsequent sorting to a precise destination within the cell.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Endoplasmic Reticulum / metabolism
  • Membrane Proteins / metabolism*
  • Microscopy, Fluorescence
  • Molecular Sequence Data
  • Mutagenesis
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Sequence Homology, Amino Acid
  • Signal Transduction*
  • Subcellular Fractions / metabolism*

Substances

  • Membrane Proteins
  • Saccharomyces cerevisiae Proteins