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J. Biol. Chem., Vol. 280, Issue 32, 28944-28951, August 12, 2005

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Isoform-specific Interaction of Golgin-160 with the Golgi-associated Protein PIST^*

Stuart W. Hicks and Carolyn E. Machamer

From the Department of Cell Biology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205

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.

Received for publication, May 4, 2005 , and in revised form, June 2, 2005.

^* This work was supported by National Institutes of Health Grant GM42522 (to C. E. M.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Dept. of Cell Biology, Johns Hopkins University School of Medicine, 725 Wolfe St., Baltimore, MD 21205. Tel.: 410-955-1809; Fax: 410-955-4129; E-mail: machamer{at}jhmi.edu.

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