A direct interaction between these two proteins was observed in vitro.
Yet the mystery about the heterophilic bond between these two proteins remained unsolved.
The interface between these two proteins is composed of several mostly independent modules.
Septin 7 was detected at 49 kDA in input lysates of PBL (input PBL) as well as after immunoprecipitation of DOCK8, verifying an interaction between these two proteins.
We found that a STIM1 mutant expressing only the ER luminal domain still binds UNC93B1 indicating that the interaction between these two proteins takes place in the ER.
Furthermore, a physical interaction between these two proteins is required for AID to bind to DNA, in an RGYW-dependent manner, during T7-polymerase-mediated transcription.
DOCK8 was detected at 190 kDA in input lysates of PBL (input PBL) as well as after immunoprecipitation of ILK (B), verifying an interaction between these two proteins.
When HDAC1 activity was inhibited, MCF7 not only apparently initiated EMT but also up-regulated SNAIL, indicating the cross-talk between these two proteins.
However, the specific interactions between these two proteins and the functional importance of these interactions for the HCV viral life cycle remain unclear.
The BRCA1 wild-type protein demonstrates a 3.8-fold increase in luciferase activity in this system when co-expressed with the VP16 PALB2 fusion protein, indicating a stable interaction between these two proteins (Figure 3b).
