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RER1  -  Rer1p

Saccharomyces cerevisiae S288c

Synonyms: Protein RER1, Retention of ER proteins 1, YCL001W, YCL1W
 
 
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High impact information on RER1

  • Bsd2 also controls the vacuolar targeting of a manganese transporter and a mutant plasma membrane ATPase, and together with the ER retrieval receptor Rer1, it protects cells from stress [1].
  • We present the first evidence that Rer1p directly interacts with the transmembrane domain (TMD) of Sec12p which contains a retrieval signal [2].
  • Rer1p, a retrieval receptor for endoplasmic reticulum membrane proteins, is dynamically localized to the Golgi apparatus by coatomer [2].
  • Either a lesion of coatomer or deletion of the COOH-terminal tail of Rer1p causes its mislocalization to the vacuole [2].
  • However, the rer1 mutant is not defective in the retention of an ER-resident soluble protein, BiP, suggesting that soluble and membrane proteins are retained in the ER by distinct mechanisms [3].
 

Biological context of RER1

 

Anatomical context of RER1

  • A recessive mutation in RER1 causes mislocalization of the authentic Sec12p as well as two different Sec12 fusion proteins to the late Golgi apparatus and even to the cell surface [3].
  • The Arabidopsis thaliana RER1 gene family: its potential role in the endoplasmic reticulum localization of membrane proteins [7].
  • Thus, the Rer1p-dependent ER retrieval and the MVB sorting in late endosomes both watch polar residues in the TMD but in a different manner [8].
  • In the spo14 mutant cells, ER-like membranes were accumulated beneath the plasma membrane and the ER/Golgi shuttling protein Rer1 remained in the ER [9].
  • Furthermore, the split-ubiquitin system demonstrates that the C-terminal of Rer1p is in the cytosol [5].
 

Associations of RER1 with chemical compounds

  • Under conditions of brefeldin A treatment, human Rer1 distributes together with recycling Golgi proteins [10].
 

Other interactions of RER1

  • Pulse-chase experiments using these mutants show that alpha-COP and Rer1p function together in a very early Golgi compartment to initiate the recycling of Sec12p-derived hybrid proteins [11].
  • We demonstrate here that the transmembrane domain (TMD) of Sec71p, a type-III membrane protein, contains an ER localization signal, which is required for physical recognition by Rer1p [8].
  • Subcellular fractionation experiments indicated that the fractionation pattern of Rer1p was similar to that of an early Golgi protein, Och1p [4].
  • Furthermore, Rer1p, a retrieval receptor for ER-resident membrane proteins in the Golgi, is responsible for the TMD-dependent ER retrieval of unassembled Fet3p [12].
  • Interaction of the endoplasmic reticulum alpha 1,2-mannosidase Mns1p with Rer1p using the split-ubiquitin system [5].
 

Analytical, diagnostic and therapeutic context of RER1

  • Even in the rer1 disrupted cells, immunofluorescence of Sec12p stains the ER, implying that the retention system is still operating in the mutant [4].
  • Co-expression of NubG-Mns1p and Rer1p-Cub-protein A-lexA-VP16 in L40 yeast cells resulted in cleavage of the reporter molecule, protein A-lexA-VP16, detected by western blot analysis and by expression of beta-galactosidase activity [5].

References

  1. Bsd2 binds the ubiquitin ligase Rsp5 and mediates the ubiquitination of transmembrane proteins. Hettema, E.H., Valdez-Taubas, J., Pelham, H.R. EMBO J. (2004) [Pubmed]
  2. Rer1p, a retrieval receptor for endoplasmic reticulum membrane proteins, is dynamically localized to the Golgi apparatus by coatomer. Sato, K., Sato, M., Nakano, A. J. Cell Biol. (2001) [Pubmed]
  3. Identification of a gene required for membrane protein retention in the early secretory pathway. Nishikawa, S., Nakano, A. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  4. Membrane protein retrieval from the Golgi apparatus to the endoplasmic reticulum (ER): characterization of the RER1 gene product as a component involved in ER localization of Sec12p. Sato, K., Nishikawa, S., Nakano, A. Mol. Biol. Cell (1995) [Pubmed]
  5. Interaction of the endoplasmic reticulum alpha 1,2-mannosidase Mns1p with Rer1p using the split-ubiquitin system. Massaad, M.J., Herscovics, A. J. Cell. Sci. (2001) [Pubmed]
  6. The processing alpha1,2-mannosidase of Saccharomyces cerevisiae depends on Rer1p for its localization in the endoplasmic reticulum. Massaad, M.J., Franzusoff, A., Herscovics, A. Eur. J. Cell Biol. (1999) [Pubmed]
  7. The Arabidopsis thaliana RER1 gene family: its potential role in the endoplasmic reticulum localization of membrane proteins. Sato, K., Ueda, T., Nakano, A. Plant Mol. Biol. (1999) [Pubmed]
  8. Rer1p, a retrieval receptor for ER membrane proteins, recognizes transmembrane domains in multiple modes. Sato, K., Sato, M., Nakano, A. Mol. Biol. Cell (2003) [Pubmed]
  9. The fission yeast spo14+ gene encoding a functional homologue of budding yeast Sec12 is required for the development of forespore membranes. Nakamura-Kubo, M., Nakamura, T., Hirata, A., Shimoda, C. Mol. Biol. Cell (2003) [Pubmed]
  10. Human Rer1 is localized to the Golgi apparatus and complements the deletion of the homologous Rer1 protein of Saccharomyces cerevisiae. Füllekrug, J., Boehm, J., Röttger, S., Nilsson, T., Mieskes, G., Schmitt, H.D. Eur. J. Cell Biol. (1997) [Pubmed]
  11. Sec12p requires Rer1p for sorting to coatomer (COPI)-coated vesicles and retrieval to the ER. Boehm, J., Letourneur, F., Ballensiefen, W., Ossipov, D., Démollière, C., Schmitt, H.D. J. Cell. Sci. (1997) [Pubmed]
  12. Endoplasmic reticulum quality control of unassembled iron transporter depends on Rer1p-mediated retrieval from the golgi. Sato, M., Sato, K., Nakano, A. Mol. Biol. Cell (2004) [Pubmed]
 
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