Journal Article

Sorting Signals in the Cytosolic Tail of Plant p24 Proteins Involved in the Interaction with the COPII Coat

Inmaculada Contreras, Yaodong Yang, David G. Robinson and Fernando Aniento

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 45, issue 12, pages 1779-1786
Published in print December 2004 | ISSN: 0032-0781
Published online December 2004 | e-ISSN: 1471-9053 | DOI: http://dx.doi.org/10.1093/pcp/pch200
Sorting Signals in the Cytosolic Tail of Plant p24 Proteins Involved in the Interaction with the COPII Coat

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  • Biochemistry
  • Molecular and Cell Biology
  • Plant Sciences and Forestry

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The ability of the cytosolic tail of a plant p24 protein to bind COPI and COPII subunits from plant and animal sources in vitro has been examined. We have found that a dihydrophobic motif in the –7,–8 position (relative to the cytosolic carboxy-terminus), which strongly cooperates with a dilysine motif in the –3,–4 position for COPI binding, is required for COPII binding. In addition, we show that COPI and COPII coat proteins from plant cytosol compete for binding to the sorting motifs in these tails. Only in the absence of the dilysine motif in the –3,–4 position or after COPI depletion could we observe COPII binding to the p24 tail. This competition is not observed when using rat liver cytosol.

Keywords: Keywords: Coat protein (COP) I — COPII — p24 proteins — Plant cells — Sec23/24 dimer — Sec13/31 complex.; Abbreviations: COP, coat protein complex; GEF, guanine nucleotide exchange factor; GST, glutathione-S-transferase; IPTG, isopropylthio-β-d-galactopyranoside.

Journal Article.  6208 words.  Illustrated.

Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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