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Related Experiment Videos

Sec24 proteins and sorting at the endoplasmic reticulum.

A Pagano1, F Letourneur, D Garcia-Estefania

  • 1Department of Morphology, University Medical Center, Geneva University, Geneva CH-1211, Switzerland.

The Journal of Biological Chemistry
|March 13, 1999
PubMed
Summary

Researchers identified a family of Sec24 proteins involved in secretory vesicle formation. These proteins play a role in selecting and concentrating cargo for secretion from the endoplasmic reticulum.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Protein Trafficking

Background:

  • COPII proteins are essential for forming secretory vesicles at the endoplasmic reticulum.
  • Yeast possesses two orthologues of the Sec24 protein, a key COPII component.

Purpose of the Study:

  • To investigate the function of Sec24 orthologues in protein secretion.
  • To identify and characterize the human Sec24 protein family and their role in vesicle formation.

Main Methods:

  • Gene knock-out in yeast to study secretion defects.
  • Database searches to identify homologous proteins across species.
  • Cloning of human cDNAs encoding Sec24 homologues.
  • Co-immunoprecipitation and size exclusion chromatography to analyze protein complexes.

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  • Immunofluorescence microscopy to determine protein localization.
  • Main Results:

    • Absence of a specific Sec24 orthologue in yeast caused selective protein secretion defects.
    • A family of Sec24-related proteins exists in humans, worms, flies, and plants.
    • Two new human cDNAs encoding Sec24p homologues were identified.
    • Human Sec24 orthologues form complexes with hSec23Ap and co-localize with hSec23p and hSec13p.

    Conclusions:

    • The Sec23-24p complex is involved in cargo selection and concentration during vesicle formation.
    • Sec24 proteins are crucial for efficient protein secretion via secretory vesicles.