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Vol. 11, Issue 4, 1421-1432, April 2000

A Proline-rich Region and Nearby Cysteine Residues Target XLs to the Golgi Complex Region

Ozlem Ugur,^* and Teresa L. Z. Jones

 ^*Department of Pharmacology and Clinical Pharmacology, Medical Faculty, Ankara University, 06100 Ankara, Turkey; and  Metabolic Diseases Branch, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892

XLs is a splice variant of the heterotrimeric G protein, G_s, found on Golgi membranes in cells with regulated and constitutive secretion. We examined the role of the alternatively spliced amino terminus of XLs for Golgi targeting with the use of subcellular fractionation and fluorescence microscopy. XLs incorporated [³H]palmitate, and mutation of cysteines in a cysteine-rich region inhibited this incorporation and lessened membrane attachment. Deletion of a proline-rich region abolished Golgi localization of XLs without changing its membrane attachment. The proline-rich and cysteine-rich regions together were sufficient to target the green fluorescent protein, a cytosolic protein, to Golgi membranes. The membrane attachment and Golgi targeting of the fusion protein required the putative palmitoylation sites, the cysteine residues in the cysteine-rich region. Several peripheral membrane proteins found at the Golgi have proline-rich regions, including a G_i2 splice variant, dynamin II, III spectrin, comitin, and a Golgi SNARE, GS32. Our results suggest that proline-rich regions can be a Golgi-targeting signal for G protein  subunits and possibly for other peripheral membrane proteins as well.

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Corresponding author. E-mail address: tlzj{at}helix.nih.gov.

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Molecular Biology of the Cell
Vol. 11, 1421-1432, April 2000
Copyright © 2000 by The American Society for Cell Biology

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