High impact information on ERD2

• Mutation of this protein prevents both the HDEL receptor and a membrane protein bearing a dibasic retrieval signal from recycling to the endoplasmic reticulum [1].
• We conclude that ERD2 encodes the receptor that sorts luminal ER proteins [2].
• The ERD2 gene of Saccharomyces cerevisiae encodes the receptor which retrieves HDEL-containing containing ER proteins from the Golgi apparatus [3].
• Viable erd2 mutants have been isolated that show no obvious HDEL-dependent retention of the luminal ER protein BiP, suggesting that retrieval of HDEL proteins is not essential for growth [3].
• Sequence analysis of SED5 reveals no significant homology with ERD2 or other known genes [4].

Biological context of ERD2

• A functional assay demonstrates that the Arabidopsis homologue, unlike the mammalian protein, can complement the lethal phenotype of the erd2 deletion mutant of Saccharomyces cerevisiae, indicating that this protein may have a similar function in plants [5].

Anatomical context of ERD2

• We suggest that the absence of ERD2 causes an imbalance between membrane flow into and out of the Golgi apparatus, and that the SED gene products can compensate for this either by slowing transport from the ER or by stimulating vesicle budding from Golgi membranes [6].
• The Saccharomyces cerevisiae gene ERD2 is responsible for the retrieval of lumenal resident proteins of the endoplasmic reticulum (ER) lost to the next secretory compartment [7].

Associations of ERD2 with chemical compounds

• The ERD2 gene, which encodes the yeast HDEL (His-Asp-Glu-Leu) receptor, is essential for growth (Semenza, J. C., K. G. Hardwick, N. Dean, and H. R. B. Pelham. 1990. Cell. 61:1349-1357; Lewis, M. J., D. J. Sweet, and H. R. B. Pelham. 1990. Cell. 61:1359-1363) [4].
• We found by computer analysis that a putative yeast proteasome subunit gene named PRS3 that encodes a protein very similar to subunit C5 of rat and human proteasomes is located immediately 3' to the ERD2 gene of Saccharomyces cerevisiae [8].
• We suggest that sorting of luminal ER proteins normally occurs in the Golgi, and that the function of ERD1 is required for the correct interaction of an HDEL receptor with its ligands [9].

Other interactions of ERD2

• Analysis of many such mutants defines two genes, ERD1 and ERD2 [9].
• We conclude that IRE1 and ERD2 together maintain normal concentrations of resident proteins within the ER [7].
• SED1 was formerly identified as a multicopy suppressor of erd2, which encodes a protein involved in retrieval of luminal endoplasmic reticulum proteins from the secretory pathway [10].

References