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We first verified that SIM deletions did not affect interaction with CtBP by coimmunoprecipitation from transfected COS1 cells.
The characterization of SP domain mutations that do not affect interaction with WRP(W/Y) proteins but block cofactor-activated phosphorylation of Gro/TLE1 provided a means of assessing the role of the latter mechanism in Gro/TLE1 anti-neurogenic activity.
We have identified amino acids in a human drug efflux pump that affect interaction with substrate and protein targeting.
Deletion of the N-terminal 60 or 120 amino acids completely eliminated the binding of TRIAD1 to CUL5 but did not affect interaction with UBCH7.
Constitutively active or inactive mutations of Smo do not affect ciliary localization of Smo, nor do they affect interaction with BBS1 (Supplementary Material, Fig. S1).
It is also possible that WC1 isoforms differ in their flexibility given that full-length WC1 molecules contain inter-domain or "hinge" regions following SRCR domains 3, 8, and 10, and this could affect interaction with the TCR.
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Recent applications of this approach to both potassium channels [9] and voltage-gated calcium channels [10] has identified a number of new mutations that affect interactions with channel modifiers [4].
DGCR8 phosphorylation does not appear to significantly affect interactions with Drosha.
We hypothesised that the PY motif of RNF11 could affect interactions with Smad7.
If a parent is suffering from PND, it may affect interactions with not only the baby but the entire family.
Likewise, retraction of the important Ub C-terminus would affect interactions with most enzymes in the Ub system.
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