Emerging roles for diverse intramembrane proteases in plant biology

Zach Adam*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

21 Scopus citations


Progress in the field of regulated intramembrane proteolysis (RIP) in recent years has made its impact on plant biology as well. Although this field within plant research is still in its infancy, some interesting observations have started to emerge. Gene encoding orthologs of rhomboid proteases, site-2 proteases (S2P), presenilin/γ-secretases, and signal peptide peptidases are found in plant genomes and some of these gene products were identified in different plant cell membranes. The lack of chloroplast-located rhomboid proteases was associated with reduced fertility and aberrations in flower morphology. Mutations in homologues of S2P resulted in chlorophyll deficiency and impaired chloroplast development. An S2P was also implicated in the response to ER stress through cleavage of ER-membrane bZIP transcription factors, allowing their migration to the nucleus and activation of the transcription of BiP chaperones. Other membrane-bound transcription factors of the NAC and PHD families were also demonstrated to undergo RIP and relocalization to the nucleus. These and other new data are expected to shed more light on the roles of intramembrane proteases in plant biology in the future. This article is part of a Special Issue entitled: Intramembrane Proteases.

Original languageAmerican English
Pages (from-to)2933-2936
Number of pages4
JournalBiochimica et Biophysica Acta - Biomembranes
Issue number12
StatePublished - 2013

Bibliographical note

Funding Information:
The author would like to thank Dr. Ronit Rimon Knopf for insightful discussions over the years and Dr. Onie Tsabari for the artwork. All the work related to the subject of this article performed in the author’s lab was supported by a grant from the Israel Science Foundation .


  • Arabidopsis thaliana
  • Chloroplast
  • ER stress
  • Plant
  • Protease


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