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RER1 Rer1p

rer1, Rer1p
The protein encoded by this gene is a multi-pass membrane protein that is localized to the golgi apparatus. It is involved in the retention of endoplasmic reticulum (ER) membrane proteins in the ER and retrieval of ER membrane proteins from the early Golgi compartment to facilitate gamma-secretase complex assembly. [provided by RefSeq, Oct 2009] (from NCBI)
Top mentioned proteins: sec12, ACID, CIs, CAN, Chx10
Papers using rer1 antibodies
Rer1p competes with APH-1 for binding to nicastrin and regulates γ-secretase complex assembly in the early secretory pathway
Annaert Wim et al., In The Journal of Cell Biology, 2004
... Polyclonal anti-murine Rer1p was generated in New Zealand white rabbits using the C-terminal sequence CKRRYKGKEDVGKTFAS coupled to KLH (Pierce Chemical Co.) as the antigen (PickCell Laboratories).
Papers on rer1
Rer1p regulates the ER retention of immature rhodopsin and modulates its intracellular trafficking.
Sato et al., Maebashi, Japan. In Sci Rep, 2013
In this study, we identified Rer1p as a modulator of ER retention and rhodopsin trafficking.
Functional Redundancy and Divergence within the Arabidopsis RETICULATA-RELATED Gene Family.
Micol et al., Alacant, Spain. In Plant Physiol, 2013
Although transcripts of RE, RER1, and RER3 were mainly detected in the bundle sheath cells of expanded leaves, functional RER3:GREEN FLUORESCENT PROTEIN was visualized in the chloroplast membranes of all photosynthetic cells.
Rer1p maintains ciliary length and signaling by regulating γ-secretase activity and Foxj1a levels.
Annaert et al., Leuven, Belgium. In J Cell Biol, 2013
In this paper, we identified Rer1p as the first endoplasmic reticulum/cis-Golgi-localized membrane protein involved in ciliogenesis.
Protein quality control by Rer1p in the early secretory pathway: from mechanism to implication in Alzheimer's disease.
Annaert et al., Leuven, Belgium. In Alzheimers Res Ther, 2012
We previously identified Retrieval to ER protein 1 (Rer1p) as the first negative regulator of the stepwise assembly of γ-secretase during endoplasmic reticulum-to-Golgi transport.
Retention in endoplasmic reticulum 1 (RER1) modulates amyloid-β (Aβ) production by altering trafficking of γ-secretase and amyloid precursor protein (APP).
Kim et al., Gainesville, United States. In J Biol Chem, 2012
RESULTS: Retention in endoplasmic reticulum 1 (RER1) regulates the trafficking of γ-secretase and APP, thereby influences Aβ production.
Rsp5 ubiquitin ligase is required for protein trafficking in Saccharomyces cerevisiae COPI mutants.
Kaminska et al., Warsaw, Poland. In Plos One, 2011
The double ret1-1 rsp5-1 mutant is also more severely defective in the Golgi-to-ER trafficking compared to the single ret1-1, secreting more of the ER chaperone Kar2p, localizing Rer1p mostly to the vacuole, and increasing sensitivity to neomycin.
Endoplasmic reticulum retention of the gamma-secretase complex component Pen2 by Rer1.
Haass et al., München, Germany. In Embo Rep, 2007
Downregulation of Rer1 leads to increased surface localization of Pen2, whereas overexpression of Rer1 stabilizes unassembled Pen2. Rer1 is the first identified interaction partner of mammalian transmembrane-based retention/retrieval signals.
Rer1p competes with APH-1 for binding to nicastrin and regulates gamma-secretase complex assembly in the early secretory pathway.
Annaert et al., Leuven, Belgium. In J Cell Biol, 2007
We characterize a new interaction partner of nicastrin, the retrieval receptor Rer1p.
Predictive validity of ventilatory and lactate thresholds for cycling time trial performance.
Foster et al., Salt Lake City, United States. In Scand J Med Sci Sports, 2006
RER1 (r2=0.57),
Structure-based functional analysis reveals a role for the SM protein Sly1p in retrograde transport to the endoplasmic reticulum.
Peng et al., Göttingen, Germany. In Mol Biol Cell, 2005
For example, in cells of the novel sly1-5 mutant, transport of newly synthesized lysosomal and secreted proteins was still efficient, but the ER-resident Kar2p/BiP was missorted to the outside of the cell, and two proteins, Sed5p and Rer1p, which normally shuttle between the Golgi and the ER, failed to relocate to the ER.
An evaluation of the predictive validity and reliability of ventilatory threshold.
Foster et al., Salt Lake City, United States. In Med Sci Sports Exerc, 2004
RER1 (r = 0.75/0.74;
Resolvins, docosatrienes, and neuroprotectins, novel omega-3-derived mediators, and their aspirin-triggered endogenous epimers: an overview of their protective roles in catabasis.
Arita et al., Boston, United States. In Prostaglandins Other Lipid Mediat, 2004
The specific receptors for these novel bioactive products from omega-3 EPA and DHA are abbreviated Resolvin D receptors (i.e., ResoDR1), Resolvin E receptor (ResoER1; RER1), and neuroprotectin D receptors (NPDR), respectively, in recognition of their respective cognate ligands.
Endoplasmic reticulum quality control of unassembled iron transporter depends on Rer1p-mediated retrieval from the golgi.
Nakano et al., Saitama, Japan. In Mol Biol Cell, 2004
Furthermore, Rer1p, a retrieval receptor for ER-resident membrane proteins in the Golgi, is responsible for the TMD-dependent ER retrieval of unassembled Fet3p.
Rer1p, a retrieval receptor for ER membrane proteins, recognizes transmembrane domains in multiple modes.
Nakano et al., Wako, Japan. In Mol Biol Cell, 2003
The yeast Golgi membrane protein Rer1p is required for the retrieval of various endoplasmic reticulum (ER) membrane proteins such as Sec12p and Sec71p to the ER.
Interaction of the endoplasmic reticulum alpha 1,2-mannosidase Mns1p with Rer1p using the split-ubiquitin system.
Herscovics et al., Montréal, Canada. In J Cell Sci, 2001
The localization of Mns1p depends on retrieval from the Golgi through a mechanism that involves Rer1p.
Rer1p, a retrieval receptor for endoplasmic reticulum membrane proteins, is dynamically localized to the Golgi apparatus by coatomer.
Nakano et al., Saitama, Japan. In J Cell Biol, 2001
Rer1p, a yeast Golgi membrane protein, is required for the retrieval of a set of endoplasmic reticulum (ER) membrane proteins.
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