GCP60 preferentially interacts with a caspase-generated golgin-160 fragment

Juan Sbodio, Stuart W. Hicks, Dan Simon, Carolyn E Machamer

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish (US)
Pages (from-to)27924-27931
Number of pages8
JournalJournal of Biological Chemistry
Volume281
Issue number38
DOIs
StatePublished - Sep 22 2006

Fingerprint

Golgi Apparatus
Caspases
Head
Apoptosis
Proteins
Nuclear Localization Signals
Two-Hybrid System Techniques
Staurosporine
Aspartic Acid
Yeast
Vertebrates
Assays
Cell Survival
Cells

ASJC Scopus subject areas

  • Biochemistry

Cite this

GCP60 preferentially interacts with a caspase-generated golgin-160 fragment. / Sbodio, Juan; Hicks, Stuart W.; Simon, Dan; Machamer, Carolyn E.

In: Journal of Biological Chemistry, Vol. 281, No. 38, 22.09.2006, p. 27924-27931.

Research output: Contribution to journalArticle

Sbodio, Juan ; Hicks, Stuart W. ; Simon, Dan ; Machamer, Carolyn E. / GCP60 preferentially interacts with a caspase-generated golgin-160 fragment. In: Journal of Biological Chemistry. 2006 ; Vol. 281, No. 38. pp. 27924-27931.
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