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The C-terminal extensions found in ForJ and several other fungal and metazoan formins also probably harbor recognition sites for additional binding partners that remain to be identified.
The larger (130 kDa and higher) DISC1 species can be hypothesized to arise through DISC1 forming high binding affinity protein complexes, either as DISC1 oligomers or with protein binding partners, that remain intact under standard experimental conditions.
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There are binding partners that demonstrate preference for each of the known arrestin conformations: free, receptor-bound, and microtubule-bound.
There are no known binding partners that would interact with the periplasmic domain of AmtB.
These co-factors can have other binding partners that are themselves regulated by different signalling pathways.
Additionally, it is likely that there are other binding partners that vary with cell type and environmental conditions.
Likely it requires binding partners that aid in vesicle nucleation, localization, targeting and recycling.
However, it is likely that further UBE2QL1 binding partners remain to be identified and their role in RCC tumorigenesis elucidated.
We identified p33ING1 as a binding partner that interacts with CSIG.
This suggests that other binding partners exist that could modulate the IKK complex activity and function.
The deficit of one binding partner leaves the remaining partners in (relative) excess.
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