Fig. 5: Intrinsic intertwining of discrete NPF networks.
From: The non-catalytic DNA polymerase ε subunit is an NPF motif recognition protein
A Many proteins with NPF motifs were found to interact with multiple unrelated NPF receptors and POLE2 was found to interact with many known NPF motif-mediated partners of other known NPF receptors in the presented experiments. This suggests that instead of multiple discrete cellular NPF networks, a single one exists in cells. B To understand the determinants of specificity between EPS15 – an EH protein with three EH domains – and POLE2, a series of DONSON chimera motifs were assayed in nHU experiments against binding to both proteins. This experiment revealed the importance of flanking sequences for efficient POLE2 binding and also the importance of multivalency for EPS15 binding. Source data can be found in Supplementary Data 2, Supplementary Figs. 15, 16, and in the Source Data File.
