Table 1. List of A. thaliana ERAD components and their potential client proteins.
Protein name1 | A. thaliana name | A. thaliana Locus | ERAD substrate | References |
---|---|---|---|---|
SEL1L/HRD3 | SEL1L (HRD3A2, EBS5) | At1g18260 | BRI1-5, BRI1-9 MLO-13 SUBEX-C57Y |
(78; 127) (78; 127) (78) (56) |
HRD1/HRD1 | HRD1A HRD1B4 |
At3g16090 At1g65040 |
BRI1-9 | (127) |
OS-9, XTP3-B/YOS9 | OS9 (EBS6) | At5g35080 | BRI1-5 BRI1-9 EFR*5 SUBEX-C57Y |
(55; 128) (55; 128) (128) (56) |
EDEM1-3/HTM1 | MNS4 MNS54 |
At5g43710 At1g27520 |
BRI1-5 BRI1-9 SUBEX-C57Y |
(57) (57) (56) |
HERP/USA1 | EBS76 | At4G29960 | BRI1-9 BRI1-5 EFR*5 |
(81) (81) (81) |
UBE2J1/UBC6 | UBC32 | At3g17000 | BRI1-5 BRI1-9 MLO-123 |
(22) (22) (22) |
The names of the mammalian/yeast homologs are given.
There is another SEL1L homologue in the A. thaliana genome (HRD3B), which is a pseudogene and does not play any role in ERAD (78; 127).
MLO-1/MLO-12 are non-glycosylated ERAD-C substrates (95).
HRD1A/HRD1B and MNS4/MNS5 appear functionally redundant.
“*”Highlights that misfolded EFR (e.g. present in uggt or sdf2 mutants) is a glycan-dependent ERAD substrate.
Putative similar function like yeast USA1 and human HERP.