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. Author manuscript; available in PMC: 2020 Feb 24.
Published in final edited form as: Annu Rev Plant Biol. 2018 Mar 23;69:147–172. doi: 10.1146/annurev-arplant-042817-040331

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)
1

The names of the mammalian/yeast homologs are given.

2

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).

3

MLO-1/MLO-12 are non-glycosylated ERAD-C substrates (95).

4

HRD1A/HRD1B and MNS4/MNS5 appear functionally redundant.

5

“*”Highlights that misfolded EFR (e.g. present in uggt or sdf2 mutants) is a glycan-dependent ERAD substrate.

6

Putative similar function like yeast USA1 and human HERP.