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J. Biol. Chem., Vol. 281, Issue 38, 27924-27931, September 22, 2006

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GCP60 Preferentially Interacts with a Caspase-generated Golgin-160 Fragment^*

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

Golgin-160, a ubiquitous protein in vertebrates, localizes to the cytoplasmic face of the Golgi complex. Golgin-160 has a large coiled-coil C-terminal domain and a non-coiled-coil N-terminal ("head") domain. The head domain contains important motifs, including a nuclear localization signal, a Golgi targeting domain, and three aspartates that are recognized by caspases during apoptosis. Some of the caspase cleavage products accumulate in the nucleus when overexpressed. Expression of a non-cleavable form of golgin-160 impairs apoptosis induced by some pro-apoptotic stimuli; thus cleavage of golgin-160 appears to play a role in apoptotic signaling. We used a yeast two-hybrid assay to screen for interactors of the golgin-160 head and identified GCP60 (Golgi complex-associated protein of 60 kDa). Further analysis demonstrated that GCP60 interacts preferentially with one of the golgin-160 caspase cleavage fragments (residues 140–311). This strong interaction prevented the golgin-160 fragment from accumulating in the nucleus when this fragment and GCP60 were overexpressed. In addition, cells overexpressing GCP60 were more sensitive to apoptosis induced by staurosporine, suggesting that nuclear-localized golgin-160-(140–311) might promote cell survival. Our results suggest a potential mechanism for regulating the nuclear translocation and potential functions of golgin-160 fragments.

Received for publication, April 6, 2006 , and in revised form, July 5, 2006.

^* 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.

¹ Present address: Section of Microbial Pathogenesis, Yale University School of Medicine, New Haven, CT 06536.

² 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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