| First Author | Peterson TA | Year | 2013 |
| Journal | Biochim Biophys Acta | Volume | 1833 |
| Issue | 3 | Pages | 487-93 |
| PubMed ID | 23195223 | Mgi Jnum | J:198864 |
| Mgi Id | MGI:5499677 | Doi | 10.1016/j.bbamcr.2012.11.011 |
| Citation | Peterson TA, et al. (2013) ARF1-regulated coatomer directs the steady-state localization of protein kinase C epsilon at the Golgi apparatus. Biochim Biophys Acta 1833(3):487-93 |
| abstractText | Protein kinase C epsilon (PKCepsilon) contributes to multiple signaling pathways affecting human disease. The function of PKCepsilon requires it to undergo changes in subcellular distribution in response to signaling events. While the mechanisms underlying this translocation are incompletely understood, it involves the receptor for activated C kinase protein (RACK2/beta'-COP). This receptor also functions as a vesicle coat protein in the secretory pathway where it is regulated by the small GTP-binding protein ADP-ribosylation factor, ARF1. We inhibited ARF1 activation to test the requirement for RACK2/beta'-COP in PKCepsilon localization in NIH3T3 fibroblasts. We found that steady-state localization of PKCepsilon at the Golgi complex requires ARF1-regulated RACK2/beta'-COP function. By contrast, we did not observe any defects in phorbol ester-induced translocation when ARF1 was inhibited. We also found that PKCepsilon bound to isolated membranes through two distinct mechanisms. One mechanism was dependent upon RACK2/beta'-COP while a second was RACK2/beta'-COP-independent and stimulated by phorbol esters. Finally, we show that RACK2/beta'-COP affects the subcellular distribution of a constitutively active form of PKCepsilon, in a manner similar to what we observed for wild-type PKCepsilon. Together, our data support a role for RACK2/beta'-COP in the steady-state localization of PKCepsilon at the Golgi apparatus, which may be independent of its role during PKCepsilon translocation to the cell surface. |
