Insights from bacterial subtilases into the mechanisms of intramolecular chaperone-mediated activation of furin

Ujwal Shinde, Gary Thomas

Research output: Chapter in Book/Report/Conference proceedingChapter

37 Scopus citations

Abstract

Prokaryotic subtilisins and eukaryotic proprotein convertases (PCs) are two homologous protease subfamilies that belong to the larger ubiquitous super-family called subtilases. Members of the subtilase super-family are produced as zymogens wherein their propeptide domains function as dedicated intramolecular chaperones (IMCs) that facilitate correct folding and regulate precise activation of their cognate catalytic domains. The molecular and cellular determinants that modulate IMC-dependent folding and activation of PCs are poorly understood. In this chapter we review what we have learned from the folding and activation of prokaryotic subtilisin, discuss how this has molded our understanding of furin maturation, and foray into the concept of pH sensors, which may represent a paradigm that PCs (and possibly other IMC-dependent eukaryotic proteins) follow for regulating their biological functions using the pH gradient in the secretory pathway.

Original languageEnglish (US)
Title of host publicationProprotein Convertases
EditorsMajambu Mbikay, Nabil G. Seidah
Pages59-106
Number of pages48
DOIs
StatePublished - Oct 24 2011

Publication series

NameMethods in Molecular Biology
Volume768
ISSN (Print)1064-3745

Keywords

  • Intramolecular chaperones
  • histidine protonation
  • pH sensors
  • proprotein convertases
  • protease activation and regulation
  • secretory pathway
  • subtilases

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

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  • Cite this

    Shinde, U., & Thomas, G. (2011). Insights from bacterial subtilases into the mechanisms of intramolecular chaperone-mediated activation of furin. In M. Mbikay, & N. G. Seidah (Eds.), Proprotein Convertases (pp. 59-106). (Methods in Molecular Biology; Vol. 768). https://doi.org/10.1007/978-1-61779-204-5_4