PMID- 12225666
OWN - NLM
STAT- MEDLINE
DCOM- 20030616
LR  - 20190728
IS  - 0960-9822 (Print)
IS  - 0960-9822 (Linking)
VI  - 12
IP  - 17
DP  - 2002 Sep 3
TI  - Conservation of intramembrane proteolytic activity and substrate specificity in 
      prokaryotic and eukaryotic rhomboids.
PG  - 1507-12
AB  - Rhomboid is an intramembrane serine protease responsible for the proteolytic 
      activation of Drosophila epidermal growth factor receptor (EGFR) ligands. 
      Although nothing is known about the function of the approximately 100 currently 
      known rhomboid genes conserved throughout evolution, a recent analysis suggests 
      that a Rhomboid from the pathogenic bacterium Providencia stuartii is involved in 
      the production of a quorum-sensing factor. This suggests that an intercellular 
      signaling mechanism may have been conserved between prokaryotes and metazoans. 
      However, the function of prokaryotic Rhomboids is unknown. We have examined the 
      ability of eight prokaryotic Rhomboids to cleave the three Drosophila EGFR 
      ligands. Despite their striking sequence divergence, Rhomboids from one 
      Gram-positive and four Gram-negative species, including Providencia, specifically 
      cleaved Drosophila substrates, but not similar proteins such as Transforming 
      Growth Factor alpha (TGFalpha) and Delta. Although the sequence similarity 
      between these divergent Rhomboids is very limited, all contain the putative 
      serine catalytic triad residues, and their specific mutation abolished protease 
      activity. Therefore, despite low overall homology, the Rhomboids are a family of 
      ancient, functionally conserved intramembrane serine proteases, some of which 
      also have conserved substrate specificity. Moreover, a function for Rhomboids in 
      activating intercellular signaling appears to have evolved early.
FAU - Urban, Sinisa
AU  - Urban S
AD  - MRC Laboratory of Molecular Biology, Cambridge, CB2 2QH, United Kingdom.
FAU - Schlieper, Daniel
AU  - Schlieper D
FAU - Freeman, Matthew
AU  - Freeman M
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Curr Biol
JT  - Current biology : CB
JID - 9107782
RN  - 0 (Bacterial Proteins)
RN  - 0 (Drosophila Proteins)
RN  - 0 (Escherichia coli Proteins)
RN  - 0 (Intracellular Signaling Peptides and Proteins)
RN  - 0 (Krn protein, Drosophila)
RN  - 0 (Ligands)
RN  - 0 (Membrane Proteins)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Repressor Proteins)
RN  - 0 (Rho protein, Drosophila)
RN  - 0 (Transforming Growth Factor alpha)
RN  - 0 (aarA protein, Providencia stuartii)
RN  - 0 (delta protein)
RN  - 0 (grk protein, Drosophila)
RN  - 148175-53-5 (spi protein, Drosophila)
RN  - 62229-50-9 (Epidermal Growth Factor)
RN  - 76057-06-2 (Transforming Growth Factors)
RN  - EC 2.7.10.1 (ErbB Receptors)
RN  - EC 3.4.21.- (Serine Endopeptidases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Bacterial Proteins/*metabolism
MH  - Cells, Cultured
MH  - Drosophila Proteins/*metabolism
MH  - Drosophila melanogaster/*enzymology
MH  - *Epidermal Growth Factor
MH  - ErbB Receptors/physiology
MH  - Escherichia coli Proteins/metabolism
MH  - Gram-Negative Bacteria/enzymology
MH  - Gram-Positive Bacteria/enzymology
MH  - Intracellular Signaling Peptides and Proteins
MH  - Ligands
MH  - Mammals
MH  - Membrane Proteins/*metabolism
MH  - Molecular Sequence Data
MH  - Providencia/*enzymology
MH  - Recombinant Fusion Proteins/metabolism
MH  - Repressor Proteins/*physiology
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
MH  - Serine Endopeptidases/*metabolism
MH  - Signal Transduction/physiology
MH  - Species Specificity
MH  - Substrate Specificity
MH  - Transforming Growth Factor alpha/*metabolism
MH  - Transforming Growth Factors/*metabolism
EDAT- 2002/09/13 10:00
MHDA- 2003/06/17 05:00
CRDT- 2002/09/13 10:00
PHST- 2002/09/13 10:00 [pubmed]
PHST- 2003/06/17 05:00 [medline]
PHST- 2002/09/13 10:00 [entrez]
AID - S0960-9822(02)01092-8 [pii]
AID - 10.1016/s0960-9822(02)01092-8 [doi]
PST - ppublish
SO  - Curr Biol. 2002 Sep 3;12(17):1507-12. doi: 10.1016/s0960-9822(02)01092-8.