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Human Molecular Genetics, 1999, Vol. 8, No. 7 1263-1269
© 1999 Oxford University Press

Presenilins interact with Rab11, a small GTPase involved in the regulation of vesicular transport

Cécile Dumanchin1, Christian Czech2, Dominique Campion1, Marie Hélène Cuif3, Thomas Poyot2, Cosette Martin1, Françoise Charbonnier1, Bruno Goud3, Laurent Pradier2 and Thierry Frebourg1,a

1INSERM EPI 9906, Faculté de Médecine et de Pharmacie, 22 Boulevard de Gambetta, 76183 Rouen and IFRMP, Mont-Saint-Aignan, 76821 Rouen Cedex, France, 2Rhone Poulenc Rorer, Centre de Recherche de Vitry-Alfortville, 94403 Vitry-sur-Seine Cedex, France and 3Unité Mixte de Recherche CNRS 144, Institut Curie, 75248 Paris Cedex 05, France

Presenilin 1 (PS1) mutations account for the majority of early-onset dominant cases of familial Alzheimer’s disease. Presenilins (PSs) are located in many intra­cellular compartments such as the endoplasmic reticulum, Golgi apparatus, nuclear region and vesicular structures. These proteins include from seven to nine putative transmembrane domains, with the N- and C-terminal ends and a large hydrophilic loop orientated towards the cytoplasm. We report an interaction between the human PS1 or PS2 hydrophilic loop and Rab11, a small GTPase belonging to the Ras-related superfamily. Interaction domains were mapped to codons 374–400 for PS1 and to codons 106–179 for Rab11, a region including the fourth GTP-binding domain. Considering the implication of Rab proteins in vesicular transport pathways, the PS–Rab11 inter­action suggests that PSs might be involved in amyloid precursor protein vesicular routing.

a To whom correspondence should be addressed. Tel: +33 2 32 88 81 82; Fax: +33 2 32 88 80 80; Email: frebourg{at}chu-rouen.fr


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