Plant Cell Journal of Pharmacology and Experimental Therapeutics
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First published online May 2, 2002; 10.1105/tpc.000620

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The Plant Cell, Vol. 14, 1077-1092, May 2002, Copyright © 2002,
American Society of Plant Biologists

The Destination for Single-Pass Membrane Proteins Is Influenced Markedly by the Length of the Hydrophobic Domain

Federica Brandizzia, Nathalie Frangneb, Sophie Marc-Martinc, Chris Hawesa, Jean-Marc Neuhausc and Nadine Paris1,2,c

a Research School of Biological and Molecular Sciences, Oxford Brookes University, Gipsy Lane Campus, OX3 0BP Headington-Oxford, United Kingdom
b Unité Mixte de Recherche 5667, Reproduction et Développement des Plantes, 46 allée d'Italie, F-69364 Lyon, France
c Laboratoire de Biochimie, Emile-Argand 9, CH-2007 Neuchâtel, Switzerland

2 To whom correspondence should be addressed. E-mail nadine.paris{at}univ-rouen.fr; fax 33-235146787

The tonoplast was proposed as a default destination of membrane-bound proteins without specific targeting signals. To investigate the nature of this targeting, we created type I fusion proteins with green fluorescent protein followed by the transmembrane domain of the human lysosomal protein LAMP1. We varied the length of the transmembrane domain from 23 to either 20 or 17 amino acids by deletion within the hydrophobic domain. The resulting chimeras, called TM23, TM20, and TM17, were expressed either transiently or stably in tobacco. TM23 clearly accumulated in the plasmalemma, as confirmed by immunoelectron microscopy. In contrast, TM17 clearly was retained in the endoplasmic reticulum, and TM20 accumulated in small mobile structures. The nature of the TM20-labeled compartments was investigated by coexpression with a marker localized mainly in the Golgi apparatus, AtERD2, fused to a yellow fluorescent protein. The strict colocalization of both fluorescent proteins indicated that TM20 accumulated in the Golgi apparatus. To further test the default destination of type I membrane proteins, green fluorescent protein was fused to the 19–amino acid transmembrane domain of the plant vacuolar sorting receptor BP-80. The resulting chimera also accumulated in the Golgi instead of in post-Golgi compartments, where native BP-80 localized. Additionally, when the transmembrane domain of BP-80 was lengthened to 22 amino acids, the reporter escaped the Golgi and accumulated in the plasma membrane. Thus, the tonoplast apparently is not a favored default destination for type I membrane proteins in plants. Moreover, the target membrane where the chimera concentrates is not unique and depends at least in part on the length of the membrane-spanning domain.




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