Disruption of interface-2 with stomatin R97D led to an intermediate phenotype so that ASIC3 proton-gated current amplitudes at both pH 4.0 and pH 6.0 were not significantly different from wild-type ASIC3 alone or ASIC3 co-expressed with stomatin.
This zero time point S181 phosphorylation is also observed for the full-length IKK2 bearing the I413A/L414A V-shaped interface mutations, suggesting that disruption of this interface is not sufficient to impede activation loop phosphorylation when IKK2 is overexpressed in Sf9 insect cells.
The integration of a temperature-responsive polymer on the electrode surface enables easy manipulation of the biological sensing interface (i.e., addition of biotin, streptavidin, and antibody), thus allowing for temperature-induced regeneration and disruption of the interface architecture of the electrode surface.
Disruption of this interface inhibits the downstream events critical for chronic myelogenous leukemia signaling.
Disruption of the interface generated either soluble tetramers or putative dimers that were absolutely insoluble and inactive.
In contrast, the adhesion-blocking antibody, ASC-8, caused disruption of this interface as evidenced by a split seen just below the basal keratinocytes between epidermis and dermis.
We show that disruption of this interface completely abolishes Bcr-Abl leukemogenicity.
Disruption of this interface abolished the development of CML in a mouse bone marrow transplantation model and enhanced TKI sensitivity of nonmutated and TKI-resistant Bcr-Abl forms.
Disruption of this interface led to inhibition of downstream events critical for CML signaling and, importantly, completely abolished leukemia formation in mice.
These data suggest that full Abl activity requires the observed I164-mediated interaction of the SH2 domain with the kinase domain and that disruption of this interface severely compromises phosphorylation of Abl substrates in cells.
This suggests that the trigger for subunit exchange does not involve the disruption of the interface between the kinase domain and the hub that is seen in the structure of the autoinhibited holoenzyme.
