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ADP-ribosylation factor is functionally and physically associated with the Golgi complex.

T Stearns1, M C Willingham, D Botstein

  • 1Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.

Proceedings of the National Academy of Sciences of the United States of America
|February 1, 1990
PubMed
Summary
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ADP-ribosylation factor (ARF) is crucial for intracellular protein transport. Yeast studies reveal ARF

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • ADP-ribosylation factor (ARF) is a conserved GTP-binding protein.
  • Its in vivo function remained largely unknown despite in vitro characterization.

Purpose of the Study:

  • Investigate the in vivo function of ARF using Saccharomyces cerevisiae.
  • Determine ARF's role in cellular processes, particularly protein transport.

Main Methods:

  • Generated yeast strains with an arf1 null mutation.
  • Analyzed phenotypes related to protein secretion and glycosylation.
  • Conducted genetic interaction studies with secretory pathway genes.
  • Utilized immunofluorescence and immunoelectron microscopy in mammalian cells.

Related Experiment Videos

Main Results:

  • Yeast arf1 null mutants exhibited defects in the secretory pathway, including impaired invertase glycosylation and accumulation.
  • ARF1 genetically interacted with YPT1, a gene involved in the secretory pathway.
  • ARF protein localized to the Golgi apparatus, specifically cis-Golgi membranes, in mammalian cells.

Conclusions:

  • ARF plays a vital role in intracellular protein transport to or within the Golgi apparatus.
  • This function is distinct from its previously characterized in vitro biochemical activities.