The transcription factor MYC (also c-Myc) induces histone modification, 
chromatin remodeling, and the release of paused RNA polymerase to broadly 
regulate transcription. MYC is subject to a series of post-translational 
modifications that affect its stability and oncogenic activity, but how these 
control MYC's function on the genome is largely unknown. Recent work 
demonstrates an intimate connection between nuclear compartmentalization and 
gene regulation. Here, we report that Ser62 phosphorylation and PIN1-mediated 
isomerization of MYC dynamically regulate the spatial distribution of MYC in the 
nucleus, promoting its association with the inner basket of the nuclear pore in 
response to proliferative signals, where it recruits the histone 
acetyltransferase GCN5 to bind and regulate local gene acetylation and 
expression. We demonstrate that PIN1-mediated localization of MYC to the nuclear 
pore regulates MYC target genes responsive to mitogen stimulation that are 
involved in proliferation and migration pathways. These changes are also present 
at the chromatin level, with an increase in open regulatory elements in response 
to stimulation that is PIN1-dependent and associated with MYC chromatin binding. 
Taken together, our study indicates that post-translational modification of MYC 
controls its spatial activity to optimally regulate gene expression in response 
to extrinsic signals in normal and diseased states.