Cell and Tissue Research

, Volume 351, Issue 2, pp 301–307

Rhomboid proteins: a role in keratinocyte proliferation and cancer

  • Sarah L. Etheridge
  • Matthew A. Brooke
  • David P. Kelsell
  • Diana C. Blaydon
Review

DOI: 10.1007/s00441-012-1542-1

Cite this article as:
Etheridge, S.L., Brooke, M.A., Kelsell, D.P. et al. Cell Tissue Res (2013) 351: 301. doi:10.1007/s00441-012-1542-1

Abstract

The Rhomboids represent a relatively recently discovered family of proteins, consisting in a variety of intramembrane serine proteases and their inactive homologues, the iRhoms. Rhomboids typically contain six or seven transmembrane domains (TMD) and have been classified into four subgroups: Secretase A and B, Presenilin-Associated-Rhomboid-Like (PARL) and iRhoms. Although the iRhoms, iRhom1 and iRhom2, have lost their protease activity during evolution, they retain key non-protease functions and have been implicated in the regulation of epidermal growth factor (EGF) signalling. EGF is moreover a substrate of RHBDL2, their active Rhomboid relative. Other substrates of RHBDL2 include members of the EphrinB family and thrombomodulin. RHBDL2 has also previously been demonstrated to be important in wound healing in cutaneous keratinocytes through the cleavage of thrombomodulin. Additional roles for these intriguing proteins seem likely to be revealed in the future. This review focuses on our current understanding of Rhomboids and, in particular, on RHBDL2 and iRhom2 and their roles in cellular processes and human disease.

Keywords

Rhomboid proteins iRhom2 Tylosis EGFR signalling ADAM17 

Copyright information

© Springer-Verlag Berlin Heidelberg 2012

Authors and Affiliations

  • Sarah L. Etheridge
    • 1
  • Matthew A. Brooke
    • 1
  • David P. Kelsell
    • 1
  • Diana C. Blaydon
    • 1
  1. 1.Centre for Cutaneous Research, Blizard InstituteBarts and the London School of Medicine and Dentistry, Queen Mary University of LondonLondonUK

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