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Related Experiment Videos

Structural elements that direct specific processing of different mammalian subtilisin-like prohormone convertases

A Zhou1, L Paquet, R E Mains

  • 1Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.

The Journal of Biological Chemistry
|September 15, 1995
PubMed
Summary

Prohormone convertases PC1 and PC2 are crucial for processing proopiomelanocortin (POMC). Structural elements, particularly the proregion and C-terminus, dictate PC1 and PC2 processing and function.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Subtilisin-like prohormone convertases (PCs), including PC1 and PC2, are essential endoproteases.
  • These enzymes sequentially process proopiomelanocortin (POMC) and other precursor proteins.
  • Understanding the structural determinants of PC processing is key to elucidating their biological roles.

Purpose of the Study:

  • To investigate the structural elements that direct the differential processing of PC1 and PC2.
  • To determine the role of specific domains, such as the proregion and C-terminus, in PC maturation and activity.
  • To assess the impact of PC mutations and chimeras on POMC processing.

Main Methods:

  • Construction and expression of mutant and chimeric PC1 and PC2 proteins.

Related Experiment Videos

  • Utilized cell lines with distinct endogenous PC expression patterns (AtT-20, hEK293, hLoVo).
  • Analyzed proregion cleavage, secretion, oligosaccharide maturation, and POMC processing.

    • Main Results:

    • COOH-terminally truncated PC1 showed efficient proregion cleavage and secretion, unlike an active-site mutant.
    • Proregion substitution with furin enabled PC1 cleavage, but a furin/PC2 chimera showed low efficiency.
    • Swapping PC1 and PC2 proregions resulted in failure to cleave, impaired maturation, and ER retention.

    Conclusions:

    • The COOH-terminus of PC1 influences its routing and storage.
    • PC proregions are replaceable in a molecule-specific manner, and their removal is critical for routing and activity.
    • The precise role of the oxyanion hole in PC2 remains undetermined.