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Published on: August 4, 2019

p53/58 binds COPI and is required for selective transport through the early secretory pathway

E J Tisdale1, H Plutner, J Matteson

  • 1The Scripps Research Institute, Department of Cell Biology, La Jolla, California 92037, USA.

The Journal of Cell Biology
|May 5, 1997
PubMed

Insights

A novel antibody targeting p53/58 protein blocks anterograde transport, revealing its role in protein trafficking and coat exchange between ER and Golgi. This impacts understanding of vesicular transport dynamics.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Protein Trafficking

Background:

  • p53/58 is a transmembrane protein involved in the endoplasmic reticulum (ER) to Golgi transport pathway.
  • It cycles between the ER and pre-Golgi intermediates, specifically vesicular-tubular clusters (VTCs).

Purpose of the Study:

  • To investigate the function of p53/58 in protein transport using a newly developed antibody.
  • To elucidate the role of the p53/58 cytoplasmic tail in retrograde transport and coat protein recruitment.

Main Methods:

  • Generation of a specific antibody targeting the p53/58 cytoplasmic tail.
  • Analysis of anterograde transport of viral glycoproteins in the presence of the antibody.
  • Assessment of COPI coat recruitment to p53/58-containing membranes.

Main Results:

  • The antibody against p53/58's cytoplasmic tail arrested anterograde transport of viral glycoproteins.
  • p53/58 accumulated in pre-Golgi intermediates (VTCs).
  • Antibody binding inhibited COPI coat recruitment, implicating the KKXX motif in retrograde traffic.

Conclusions:

  • p53/58 plays a crucial role in regulating protein transport between the ER and Golgi.
  • Its function is essential for the exchange of COPII and COPI coats during protein segregation.
  • This suggests p53/58 is a key regulator in the coupled anterograde and retrograde protein trafficking pathways.

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