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Published online 17 June 2002. doi:10.1083/jcb.200202022
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© The Rockefeller University Press, 0021-9525/2002/6/1197 $5.00
The Journal of Cell Biology, Volume 157, Number 7, June 24, 2002 1197-1209

Article

Modulation of receptor cycling by neuron-enriched endosomal protein of 21 kD



Pascal Steiner1,2, J.-C. Floyd Sarria1,2, Liliane Glauser1,2, Sarah Magnin1,2, Stefan Catsicas1 and Harald Hirling1,2

1 Faculté des Sciences de la Vie, Ecole Polytechnique Fédérale de Lausanne, 1015 Lausanne, Switzerland
2 Institut de Biologie Cellulaire et de Morphologie, 1005 Lausanne, Switzerland

Address correspondence to Harald Hirling, Faculté des Sciences de la Vie, EPFL, Lausanne 1015, Switzerland. Tel.: 41-21-693-5363. Fax: 41-21-693-5369. E-mail: harald.hirling{at}epfl.ch

Although correct cycling of neuronal membrane proteins is essential for neurite outgrowth and synaptic plasticity, neuron-specific proteins of the implicated endosomes have not been characterized. Here we show that a previously cloned, developmentally regulated, neuronal protein of unknown function binds to syntaxin 13. We propose to name this protein neuron-enriched endosomal protein of 21 kD (NEEP21), because it is colocalized with transferrin receptors, internalized transferrin (Tf), and Rab4. In PC12 cells, NEEP21 overexpression accelerates Tf internalization and recycling, whereas its down-regulation strongly delays Tf recycling. In primary neurons, NEEP21 is localized to the somatodendritic compartment, and, upon N-methyl-D-aspartate (NMDA) stimulation, the alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionate receptor subunit GluR2 is internalized into NEEP21-positive endosomes. NEEP21 down-regulation retards recycling of GluR1 to the cell surface after NMDA stimulation of hippocampal neurons. In summary, NEEP21 is a neuronal protein that is localized to the early endosomal pathway and is necessary for correct receptor recycling in neurons.

Key Words: recycling; SNARE; transferrin; development; 1A75


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