Investigations of binding of the scaffold protein PICK1 to transmembrane proteins in their native membrane environment demonstrate potent but slow dynamics and reveal distinct binding modes supporting different biological functions.
The motor that drives preproteins into the mitochondrial matrix is coupled to the translocase by Tim44, a two-domain scaffold protein with an intrinsically disordered "dynamic arm" and a structurally stable anchoring domain.
A newly identified component in the architecture of the axon/myelin-unit – the septin/anillin scaffold – maintains the structure of myelin in the central nervous system, thereby preventing myelin outfoldings.
Structural and biochemical analyses of BRCT domain interactions defines TOPBP1/Rad4 selectivity for phosphorylated motifs, allowing identification of new interactions, and providing insights into assembly of different TOPBP1-scaffolded DNA repair complexes.
Biochemical and structural studies uncover an unexpected mode of interaction, with unprecedented high affinity, between INAD scaffold and NORPA that is critical for Drosophila compound eye photo-transduction.
Components of the nuclear pore complex share structural and functional features with soluble nuclear transport receptors, which suggests that there may be an evolutionary relationship between these two types of protein.