Conversion of a secretory protein into a transmembrane protein results in its transport to the Golgi complex but not to the cell surface

Cell. 1984 Jul;37(3):779-87. doi: 10.1016/0092-8674(84)90413-6.

Abstract

We have carried out experiments designed to ask if it is possible to convert a secretory protein into an integral membrane protein by appending the membrane spanning domain of an integral membrane protein to its carboxy terminus. We first obtained expression of a cDNA clone encoding rat growth hormone (rGH) in eucaryotic cells, and found that this protein was secreted. We then constructed and expressed a hybrid gene encoding rGH fused to the membrane spanning and cytoplasmic domains of the vesicular stomatitis virus (VSV) glycoprotein (G). This fusion protein was anchored in microsomal membranes in the expected transmembrane configuration. The fusion protein was transported to the Golgi apparatus, and was esterified to palmitic acid, but it was not transported to the cell surface. We suggest that the sorting signal which allows rapid secretion of soluble rGH does not function when the protein is bound to the membrane.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Biological Transport
  • Cell Compartmentation
  • Genetic Engineering
  • Golgi Apparatus / metabolism*
  • Growth Hormone / genetics
  • Growth Hormone / metabolism*
  • Intracellular Membranes / metabolism
  • Membrane Glycoproteins*
  • Membrane Proteins / metabolism*
  • Palmitic Acid
  • Palmitic Acids / metabolism
  • Rats
  • Viral Envelope Proteins*
  • Viral Proteins / metabolism*

Substances

  • G protein, vesicular stomatitis virus
  • Membrane Glycoproteins
  • Membrane Proteins
  • Palmitic Acids
  • Viral Envelope Proteins
  • Viral Proteins
  • Palmitic Acid
  • Growth Hormone