Fragmentation of a Golgi-localized chimeric protein allows detergent solubilization and reveals an alternate conformation of the cytoplasmic domain

Biochemistry
C S Sevier, Carolyn E Machamer

Abstract

Golgi resident proteins maintain their localization despite a continual protein and lipid flux through the organelle. To study Golgi retention mechanisms, we have focused upon the chimeric protein Gm1. This protein contains the Golgi transmembrane domain targeting signal from the infectious bronchitis virus M protein and the lumenal and cytoplasmic domain of the vesicular stomatitis virus glycoprotein (VSV G). The Gm1 protein is targeted to the Golgi where it forms an unusually stable detergent-resistant oligomer. The formation of oligomeric structures may aid retention of Golgi resident proteins. Thus, determining the stabilization mechanism may shed light on Golgi protein retention. Previous work determined that the transmembrane domain is required for the targeting and oligomerization of Gm1, but it is the cytoplasmic tail that stabilizes the complexes [Weisz, O. A., Swift, A. M., and Machamer, C. E. (1993) J. Cell Biol. 122, 1185-1196]. However, further study of the oligomer has been difficult due to its insolubility. Here we report that fragmenting the Gm1 protein into several pieces facilitates solubilization by sodium dodecyl sulfate (SDS). By analyzing the fragments produced after cleavage, we determined that the stabil...Continue Reading

References

Oct 1, 1991·The Journal of Cell Biology·A M Swift, C E Machamer
Jan 1, 1987·Annual Review of Biochemistry·S R Pfeffer, J E Rothman
Jan 1, 1985·Annual Review of Cell Biology·M G Farquhar
Jul 1, 1974·European Journal of Biochemistry·W M Bonner, R A Laskey
Sep 1, 1993·The Journal of Cell Biology·O A WeiszC E Machamer

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Citations

Dec 29, 1998·The Journal of Biological Chemistry·D L MarksR E Pagano

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