Core principles of intramembrane proteolysis: comparison of rhomboid and site-2 family proteases

Sinisa Urban, Yigong Shi

Research output: Contribution to journalArticle

Abstract

Cleavage of proteins within their membrane-spanning segments is an ancient regulatory mechanism that has evolved to control a myriad of cellular processes in all forms of life. Although three mechanistic families of enzymes have been discovered that catalyze hydrolysis within the water-excluding environment of the membrane, how they achieve this improbable reaction has been both a point of controversy and skepticism. The crystal structures of rhomboid and site-2 protease, two different classes of intramembrane proteases, have been solved recently. Combined with current biochemical analyses, this advance provides an unprecedented view of how nature has solved the problem of facilitating hydrolysis within membranes in two independent instances. We focus on detailing the similarities between these unrelated enzymes to define core biochemical principles that govern this conserved regulatory mechanism.

Original languageEnglish (US)
Pages (from-to)432-441
Number of pages10
JournalCurrent Opinion in Structural Biology
Volume18
Issue number4
DOIs
StatePublished - Aug 2008

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Proteolysis
Peptide Hydrolases
Membranes
Hydrolysis
Enzymes
Water
Proteins

ASJC Scopus subject areas

  • Molecular Biology
  • Structural Biology

Cite this

Core principles of intramembrane proteolysis : comparison of rhomboid and site-2 family proteases. / Urban, Sinisa; Shi, Yigong.

In: Current Opinion in Structural Biology, Vol. 18, No. 4, 08.2008, p. 432-441.

Research output: Contribution to journalArticle

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