Golgin-160 belongs to the golgin family of Golgi-localized proteins, which have been implicated in Golgi structure and function. Golgin-160 possesses an N-terminal non-coiled-coil "head" domain followed by an extensive coiled-coil region. Using the N-terminal head domain of golgin-160 as bait in a yeast two-hybrid screen, the postsynaptic density-95/Discs large/zona occludens-1 (PDZ) domain protein interacting specifically with TC10 (PIST) was identified to interact with golgin-160. PIST (also known as GOPC, CAL, and FIG) has been implicated in the trafficking of a subset of plasma membrane proteins, supporting a role of golgin-160 in vesicular trafficking. Golgin-160 and PIST colocalize to Golgi membranes and interact in vivo. Glutathione S-transferase binding experiments identified an internal region of PIST that includes a coiled-coil domain, which interacts directly with golgin-160. Similar binding experiments identified a leucine-rich repeat within golgin-160 necessary for interaction with PIST. Therefore, our data suggest that golgin-160 may participate in PIST-dependent trafficking of cargo. Interestingly, we also discovered a widely expressed isoform of golgin-160, golgin-160B, which lacks the exon encoding the leucine repeat that mediates binding to PIST. As predicted, golgin-160B was unable to bind PIST. Full-length golgin-160 and golgin-160B may link distinct subsets of proteins to effect specific membrane trafficking pathways.
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