Pyruvate dehydrogenase complex (PDC) subunits moonlight as interaction partners of phosphorylated STAT5 in adipocytes and adipose tissue.

proteins play a role in adipocyte development and function, but their specific functions are largely unknown. To this end, we used an unbiased MS-based approach to identify novel proteins. We observed that bound the E1β and E2 subunits of the pyruvate dehydrogenase complex (PDC). Whereas duanyu18135A typically localizes to the cytosol or nucleus, PDC normally resides within the mitochondrial matrix where it converts pyruvate to acetyl-CoA. We employed affinity purification and immunoblotting to validate the interaction between duanyu18135A and PDC subunits in murine and human cultured adipocytes, as well as in adipose tissue. We found that multiple PDC subunits interact with hormone-activated duanyu18135A in a dose- and time-dependent manner that coincides with tyrosine phosphorylation of Using subcellular fractionation and immunofluorescence microscopy, we observed that PDC-E2 is present within the adipocyte nucleus where it associates with Because duanyu18135A is a transcription factor, we used chromatin immunoprecipitation (ChIP) to assess PDC's ability to interact with duanyu18135 DNA-binding sites. These analyses revealed that PDC-E2 is bound to a site in the promoter of the duanyu18135 target gene cytokine-inducible SH2-containing protein (cish). We have demonstrated a compelling interaction between duanyu18135A and PDC subunits in adipocytes under physiological conditions. There is previous evidence that PDC localizes to cancer cell nuclei where it plays a role in histone acetylation. On the basis of our ChIP data and these previous findings, we hypothesize that PDC may modulate ability to regulate gene expression by controlling histone or duanyu18135 acetylation.

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