Topology of amphipathic motifs mediating Golgi localization in ArfGAP1 and its splice isoforms

The Journal of Biological Chemistry
Sharon LeviD Cassel

Abstract

The interaction of the Arf1-directed GTPase-activating protein ArfGAP1 with the Golgi apparatus depends on motifs in its noncatalytic part that are unstructured in solution but are capable of folding into amphipathic helices in vitro upon interaction with poorly packed lipids. In previous studies a few hydrophobic residues that are critical for lipid binding and Golgi localization were identified, but the precise topology of the amphipathic motifs has not been determined. Here we present a detailed analysis of the Golgi targeting and in vitro folding features of the region encompassing the amphipathic motifs (residues 199-294). Point mutation analysis revealed that most hydrophobic residues within this region contribute to Golgi localization, whereas analysis by proline replacements and alanine insertions revealed that Golgi interaction depends on folding into two amphipathic helices with a short interrupting sequence. Analysis of splice isoforms containing 10-residue in-frame insertions within their first amphipathic motifs revealed that the insertion causes a truncation of the amphipathic helix that does not extend beyond the insertion sequence. Lastly, a lysine replacement mutant recently reported to bind to negatively charg...Continue Reading

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Citations

Dec 26, 2008·Molecular Biology of the Cell·Lena KliouchnikovDan Cassel
Mar 29, 2011·Annual Review of Biochemistry·Bruno Antonny
Sep 24, 2008·The Journal of Cell Biology·Richard A KahnDan Cassel
Jul 28, 2009·FEBS Letters·R BeckD Cassel
Dec 15, 2010·Biochemical and Biophysical Research Communications·Ikuko SakakuraToshio Watanabe
Mar 10, 2010·Biochemical and Biophysical Research Communications·Moran RawetDan Cassel
Nov 27, 2015·Journal of Immunology Research·Jouda GamaraSylvain G Bourgoin
Jun 21, 2011·Cellular Logistics·Rainer BeckFelix Wieland

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