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. Author manuscript; available in PMC: 2021 May 1.
Published in final edited form as: Trends Biochem Sci. 2020 Feb 28;45(5):427–439. doi: 10.1016/j.tibs.2020.01.008

Table 2:

Human DUB-E3 complexes operating on shared substrates

DUB E3 Regulatory function of complex Reference
DUB-E3 interactions that mediate ubiquitin switches or rheostats on a shared substrate
UCHL1 MDM2 UCHL1 antagonizes MDM2-mediated ubiquitylation of p53 [78]
UCHL1 TRAF6 UCHL1 antagonizes TRAF6-mediated ubiquitylation of TRAF3 [79]
USP7 TRIM27 USP7 interacts with MAGE-L2-TRIM27 to regulate WASH ubiquitylation and actin polymerization on endosomes [25]
USP9X WWP1 USP9X interacts with WWP1 to regulate DVL2 ubiquitylation and WNT signaling [32]
USP10 RNF168 USP10 interacts with RNF168 to regulate TOP2α ubiquitylation and chromatin association [80]
USP12 ITCH USP12 interacts with ITCH to regulate Notch trafficking and degradation [81, 82]
USP13 AMFR USP13 interacts with gp78 to stabilize UBL4A and promote ERAD [45]
USP15 βTrCP USP15 interacts with βTrCP to regulate the stability of β-catenin [29]
USP20 TRAF6 USP20 interacts with TRAF6 to regulate the ubiquitylation of β-arrestin2 [83] [58]
USP28 FBXW7 USP28 interacts with FBXW7 in nucleus to regulate MYC degradation [84]
USP28 RCHY1 USP28 interacts with PIRH2 to regulate CHK2 degradation in the DNA damage checkpoint [85]
USP36 FBXW7 USP36 interacts with FBXW7 in nucleoli to regulate c-MYC degradation [86]
Polyubiquitin chain editing by DUB-E3 complexes
A20 A20 A20 performs a polyubiquitin chain editing event on RIP, replacing K63-linked polymers with K48-linked polymers, targeting RIP for degradation [49]
CYLD ITCH An ITCH-CYLD complex performs a polyubiquitin chain editing event on TAK1, replacing K63-linked polymers with K48-linked polymers, targeting TAK1 for degradation [53]