IndraLab

Statements

TMED2 binds BAP1. 8 / 8
| 8
sparser
"Validation of the BAP1 COPI interaction."
| PMC
sparser
"In order to confirm the interaction between BAP1 and the heptameric COPI complex we performed AP-immunoblot experiments ( xref )."
| PMC
sparser
"To exclude that the BAP1 interaction with the COPI complex is an artifact of overexpression of the exogenous BAP1 construct, we immunoprecipitated endogenous BAP1 using different antibodies against BAP1 in cell lysate from HeLa FRT parental cells ( xref )."
| PMC
sparser
"AP-immunoblotting of GFP-COPE shows interaction of COPA as expected, however BAP1 cannot be observed which is probably due to the low levels of BAP1 that bind to the COPI complex ( xref )."
| PMC
sparser
"Although the absolute and relative amounts of COPI that interacts with BAP1 in the AP-MS is low ( xref and xref ), the interaction can still be biologically relevant and is validated with endogenous protein as seen in the immunoblot experiments ( xref )."
| PMC
sparser
"It was intriguing that BAP1 has such a sequence in its C-terminus, but our mutational analysis suggests that the interaction between BAP1 and the COPI complex is not mediated through the C-terminal KxKxx sequence in BAP1."
| PMC
sparser
"We must be absolutely sure that the BAP1-COPI interaction is not an artifact."
| PMC
sparser
"We agree with reviewer 2 that the interaction between BAP1 and the COPI complex may be a substrate interaction as evidenced by the low protein stoichiometry observed in the affinity purification (Fig 5)."
| PMC