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Published online December 31, 2007
doi:10.1083/jcb.200708107
The Journal of Cell Biology, Vol. 179, No. 7, 1497-1510
The Rockefeller University Press, 0021-9525 $30.00
© 2007 Jung et al.
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Article

 Molecular basis of synaptic vesicle cargo recognition by the endocytic sorting adaptor stonin 2

Nadja Jung1, Martin Wienisch2, Mingyu Gu3, James B. Rand4, Sebastian L. Müller5, Gerd Krause5, Erik M. Jorgensen3, Jürgen Klingauf2, and Volker Haucke1

1 Department of Membrane Biochemistry, Institute of Chemistry and Biochemistry, Freie Universität Berlin, 14195 Berlin, Germany
2 Department of Membrane Biophysics, Max-Planck-Institute for Biophysical Chemistry, 37077 Göttingen, Germany
3 Department of Biology, University of Utah, Salt Lake City, UT 84112
4 Program in Molecular, Cell and Developmental Biology, Oklahoma Medical Research Foundation, Oklahoma City, OK 73104
5 Leibniz-Institut für Molekulare Pharmakologie, 13125 Berlin, Germany

Correspondence to Volker Haucke: v.haucke{at}biochemie.fu-berlin.de

Synaptic transmission depends on clathrin-mediated recycling of synaptic vesicles (SVs). How select SV proteins are targeted for internalization has remained elusive. Stonins are evolutionarily conserved adaptors dedicated to endocytic sorting of the SV protein synaptotagmin. Our data identify the molecular determinants for recognition of synaptotagmin by stonin 2 or its Caenorhabditis elegans orthologue UNC-41B. The interaction involves the direct association of clusters of basic residues on the surface of the cytoplasmic domain of synaptotagmin 1 and a β strand within the µ–homology domain of stonin 2. Mutation of K783, Y784, and E785 to alanine within this stonin 2 β strand results in failure of the mutant stonin protein to associate with synaptotagmin, to accumulate at synapses, and to facilitate synaptotagmin internalization. Synaptotagmin-binding–defective UNC-41B is unable to rescue paralysis in C. elegans stonin mutant animals, suggesting that the mechanism of stonin-mediated SV cargo recognition is conserved from worms to mammals.

Abbreviations used in this paper: AP-2, assembly protein complex 2; CLASP, clathrin-associated sorting protein; HEK, human embryonic kidney; µHD, µ–homology domain; NIE, neuroimmune endocrine; SV, synaptic vesicle; WT, wild type.


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