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RCE1 Rce1p

Rce1, Rce1p
This gene encodes an integral membrane protein which is classified as a member of the metalloproteinase family. This enzyme is thought to function in the maintenance and processing of CAAX-type prenylated proteins. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ZMPSTE24, ACID, CAN, HAD, STEP
Papers on Rce1
Divergent roles of CAAX motif-signaled posttranslational modifications in the regulation and subcellular localization of Ral GTPases.
Der et al., Okazaki, Japan. In J Biol Chem, Oct 2015
Both RalA and RalB require Ras converting CAAX endopeptidase 1 (RCE1) for association with the plasma membrane, albeit not with endomembranes, and loss of RCE1 caused mislocalization as well as sustained activation of both RalA and RalB.
Genome-wide gene expression profiling of low-dose, long-term exposure of human osteosarcoma cells to bisphenol A and its analogs bisphenols AF and S.
Mašič et al., Ljubljana, Slovenia. In Toxicol In Vitro, Aug 2015
For BPAF and BPS, the 'isoprenoid biosynthetic process' was enriched (up-regulated genes: HMGCS1, PDSS1, ACAT2, RCE1, DHDDS).
USP17 is required for clathrin mediated endocytosis of epidermal growth factor receptor.
Burrows et al., Belfast, United Kingdom. In Oncotarget, 2014
More recently we reported that USP17 deubiquitinates RCE1 isoform 2 and thus regulates the processing of 'CaaX' motif proteins.
Isolation, screening, characterization, and selection of superior rhizobacterial strains as bioinoculants for seedling emergence and growth promotion of Mandarin orange (Citrus reticulata Blanco).
Talukdar et al., Imphāl, India. In Can J Microbiol, 2014
Five isolates, namely RCE1, RCE2, RCE3, RCE5, and RCE7, significantly increased shoot length, shoot dry biomass, and root dry biomass of 120-day-old seedlings over the noninoculated control.
A novel RCE1 isoform is required for H-Ras plasma membrane localization and is regulated by USP17.
Burrows et al., Belfast, United Kingdom. In Biochem J, 2014
Processing of the 'CaaX' motif found on the C-termini of many proteins, including the proto-oncogene Ras, requires the ER (endoplasmic reticulum)-resident protease RCE1 (Ras-converting enzyme 1) and is necessary for the proper localization and function of many of these 'CaaX' proteins.
[Effect of different types of cold acclimation on osmotic fragility and sphericity index of rat erythrocytes].
Babiĭchuk et al., In Ross Fiziol Zh Im I M Sechenova, 2014
More over, RCE1 (exposure temperature -12 °C, during 2 days) led to the increase in osmotic fragility, but RCE2 (exposure temperature 10 °C, during 2 days), RCE3 (exposure temperature 10 °C, during 1 month) and long-term (exposure temperature 5 °C, during 1 month) - to membrane modification without change in its osmotic fragility.
A novel proteinase, SNOWY COTYLEDON4, is required for photosynthetic acclimation to higher light intensities in Arabidopsis.
Pogson et al., Canberra, Australia. In Plant Physiol, 2013
Phylogenetic and yeast complementation analyses of SCO4-like proteins reveal that SCO4 is a member of an unknown group of higher plant-specific proteinases quite distinct from the well-described CaaX-type endopeptidases RAS Converting Enzyme1 (RCE1) and zinc metallopeptidase STE24 and lacks canonical CaaX activity.
Topology of the yeast Ras converting enzyme as inferred from cysteine accessibility studies.
Schmidt et al., Athens, United States. In Biochemistry, 2013
The Ras converting enzyme (Rce1p) is an endoprotease that is involved in the post-translational processing of the Ras GTPases and other isoprenylated proteins.
Expression of claudins -2 and -4 and cingulin is coordinated with the start of stratification and differentiation in corneal epithelial cells: retinoic acid reversibly disrupts epithelial barrier.
Castro-Muñozledo et al., Mexico. In Biol Open, 2013
We studied the expression of TJ in RCE1(5T5) cells, an in vitro model which mimics the sequential steps of rabbit corneal epithelial differentiation.
A loss-of-function mutation in the nucleoporin AtNUP160 indicates that normal auxin signalling is required for a proper ethylene response in Arabidopsis.
Larsen et al., Riverside, United States. In J Exp Bot, 2012
In support of previously reported results, the sar1-7 mutant partially restored auxin responsiveness to roots of an rce1 loss-of-function mutant, indicating that AtNUP160/SAR1 is required for proper expression of factors responsible for the repression of auxin signalling.
Photoaffinity labeling of Ras converting enzyme using peptide substrates that incorporate benzoylphenylalanine (Bpa) residues: improved labeling and structural implications.
Distefano et al., Minneapolis, United States. In Bioorg Med Chem, 2012
Rce1p catalyzes the proteolytic trimming of C-terminal tripeptides from isoprenylated proteins containing CAAX-box sequences.
RAS-converting enzyme 1-mediated endoproteolysis is required for trafficking of rod phosphodiesterase 6 to photoreceptor outer segments.
Ramamurthy et al., Morgantown, United States. In Proc Natl Acad Sci U S A, 2011
RCE1 is essential for the intracellular trafficking of PDE6 and survival of photoreceptor cells.
USP17 regulates Ras activation and cell proliferation by blocking RCE1 activity.
Johnston et al., Ireland. In J Biol Chem, 2009
USP17 modulates Ras processing and activation, at least in part, by regulating RCE1 activity
Genetic analyses of the role of RCE1 in RAS membrane association and transformation.
Young et al., Göteborg, Sweden. In Methods Enzymol, 2007
RCE1 is responsible for the endoproteolytic processing of the RAS proteins and is likely responsible for endoproteolytic processing of the vast majority of CAAX proteins.
Mutational analysis of the ras converting enzyme reveals a requirement for glutamate and histidine residues.
Schmidt et al., Athens, United States. In J Biol Chem, 2006
the ras converting enzyme requires its glutamate and histidine residues
Post-prenylation-processing enzymes as new targets in oncogenesis.
Casey et al., Durham, United States. In Nat Rev Cancer, 2005
Following prenylation, these proteins usually undergo endoproteolytic processing by the RCE1 protease and then carboxyl methylation by a unique methyltransferase known as isoprenylcysteine carboxyl methyltransferase (ICMT).
On the physiological importance of endoproteolysis of CAAX proteins: heart-specific RCE1 knockout mice develop a lethal cardiomyopathy.
Young et al., San Francisco, United States. In J Biol Chem, 2004
Hearts from heart-specific Rce1 knockout mice manifested reduced levels of both the Rce1 mRNA and CAAX endoprotease activity, and the hearts manifested an accumulation of CAAX protein substrates. Rce1 knockout mice had a dilated cardiomyopathy.
A carboxyl-terminal interaction of lamin B1 is dependent on the CAAX endoprotease Rce1 and carboxymethylation.
Vaux et al., Oxford, United Kingdom. In J Cell Biol, 2003
CAAX endoprotease Rce1 is required for lamin B1 endoproteolysis
CaaX converting enzymes.
Ashby, Richmond, United States. In Curr Opin Lipidol, 1998
Proteins that contain a carboxyl-terminal CaaX motif undergo post-translational processing involving prenylation, endoproteolysis and methylesterification. Two yeast genes, AFC1 and RCE1, which are candidates for genes encoding CaaX converting enzymes, were recently identified.
Modulation of Ras and a-factor function by carboxyl-terminal proteolysis.
Rine et al., Berkeley, United States. In Science, 1997
Two genes in Saccharomyces cerevisiae, RCE1 and AFC1, were identified that appear to be responsible for this processing.
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