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HighlightsThe protein RER1 is a protein encoded by the RER1 gene in humans. RER1 was first found in yeast and is the ER retention factor for Sec12p, Sed4p, Mns1p, Sec71p, and Sec63p. Yeast reattaches to the transmembrane domains (TMDs) of these proteins and brings them back to the ER via COPI vesicles. In addition to re-running, yeast Bsd2 appears to have a similar effect on TMD-associated ER retention factors, and they share substrates.
| Basic Information of RER1 | |
| Protein Name | Protein RER1 |
| Gene Name | RER1 |
| Aliases | |
| Organism | Homo sapiens (Human) |
| UniProt ID | O15258 |
| Transmembrane Times | 3 |
| Length (aa) | 196 |
| Sequence | MSEGDSVGESVHGKPSVVYRFFTRLGQIYQSWLDKSTPYTAVRWVVTLGLSFVYMIRVYLLQGWYIVTYALGIYHLNLFIAFLSPKVDPSLMEDSDDGPSLPTKQNEEFRPFIRRLPEFKFWHAATKGILVAMVCTFFDAFNVPVFWPILVMYFIMLFCITMKRQIKHMIKYRYIPFTHGKRRYRGKEDAGKAFAS |
RER1 is a sorting receptor localized to cis-Golgi12,13. Similar to the KDEL receptor, it binds to signals in proteins destined for transient or permanent residency in the ER. Unlike the KDEL receptor, in the TM of the target protein, it is relinked to the ER-retention/retrieval sequence. To date, the matrix that reappears in mammalian cells is a non-assembled subunit consisting of a heteromembrane protein complex of plasma membrane (PM) and a multi-channel membrane protein rhodopsin 18 and PMP. Redirected to the ER-retention/retrieval sequence exposed only in unassembled subunits, but blocked in assembled subunits. Therefore, in the early secretory pathway, RER1 is part of quality control, ensuring that only fully assembled complexes are transported to the PM.
RER1 is involved in the recovery of endoplasmic omental proteins from the early Golgi region. RER1 is an important protein that mediates the transport of proteins associated with Alzheimer's disease (AD) by ER-Golgi and significantly reduces the production of amyloid-trafficking. Mammalian RER1 is also reported to modulate other proteins, such as muscle acetylcholine receptors and Foxj1a, suggesting important roles for neuromuscular synapse and ciliary development. RER1 also appears to play an important role in ER-Golgi transport and protein regulation.RER1 may also play an important role in regulating the transport and accumulation of toxicities in the αSyn form.
Fig.1 The structure of Protein RER1.
Further study on the mechanism of RER1 and downstream effects on αSyn may produce new therapeutic targets for regulating Parkinson's disease and associated synaptic nucleoprotein disease.
The data indicate that RER1 re-run controls the assembly and transport of the main sodium channels responsible for periodic discharges in PCs, Nav 1.1 and 1.6.
These results indicate that CMT-associated PMP22 (L16P) is trapped in the ER, through the calcium-related ER retention and re-running of the early Golgi retrieval system, and to some extent by the hrd1-mediated ERAD system.
These results suggest that Rer1p regulates the retention and intracellular transport of immature or misfolded retinoids by early secretion pathways.
This study reveals that Syvn may regulate the assembly of the γ-secretase complex via the degradation of Rer1, resulting in the generation of Aβ.
To obtain the soluble and functional target protein, the versatile Magic™ membrane protein production platform in Creative Biolabs enables many flexible options, from which you can always find a better match for your particular project. Besides, aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-RER1 antibody development services.
Creative Biolabs' skillful scientists are glad to leverage our expertise and advanced technologies to help you with the member protein research. If you are interested, please feel free to contact us for more details.
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