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J. Biol. Chem., Vol. 281, Issue 22, 15182-15193, June 2, 2006

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Calcyon, a Novel Partner of Clathrin Light Chain, Stimulates Clathrin-mediated Endocytosis^*

Jiping Xiao¹, Rujuan Dai¹, Laszlo Negyessy^¶, and Clare Bergson²

From the Department of Pharmacology and Toxicology, Medical College of Georgia, Augusta, Georgia 30912, the Department of Immunology, Virginia Polytechnic University, Blacksburg, Virginia 24061, and the ^¶Neurobiology Research Group, United Research Organization of the Hungarian Academy of Sciences and Semmelweis University, Budapest H1094, Hungary

In the central nervous system, clathrin-mediated endocytosis is crucial for efficient synaptic transmission. Clathrin-coated vesicle assembly and disassembly is regulated by some 30 adaptor and accessory proteins, most of which interact with clathrin heavy chain. Using the calcyon cytosolic domain as bait, we isolated clathrin light chain in a yeast two-hybrid screen. The interaction domain was mapped to the heavy chain binding domain and C-terminal regions of light chain. Further, the addition of the calcyon C terminus stimulated clathrin self-assembly in a dose-dependent fashion. Calcyon, which is a single transmembrane protein predominantly expressed in brain, localized to vesicular compartments within pre- and postsynaptic structures. There was a high degree of overlap in the distribution of LC and calcyon in neuronal dendrites, spines, and cell bodies. Co-immunoprecipitation studies further suggested an association of calcyon with the clathrin-mediated endocytic machinery. Compared with controls, HEK293 cells overexpressing calcyon exhibited significantly enhanced transferrin uptake but equivalent levels of recycling. Conversely, transferrin uptake was largely abolished in neocortical neurons obtained from mice homozygous for a calcyon null allele, whereas recycling proceeded at wild type levels. Collectively, these data indicate a role for calcyon in clathrin-mediated endocytosis in brain.

Received for publication, January 10, 2006 , and in revised form, March 27, 2006.

^* This work was supported by National Institutes of Health Grants MH063271 and MH068789, by a National Alliance for Research on Schizophrenia and Depression Independent Investigator Award (to C. B.), and by the János Bolyai Research Scholarship of the Hungarian Academy of Sciences (to L. N.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ These authors contributed equally to this work.

² To whom correspondence should be addressed: Dept. of Pharmacology and Toxicology, Medical College of Georgia, 1459 Laney Walker Blvd., Augusta, GA 30912-2300. Tel.: 706-721-1926; Fax: 706-721-2347; E-mail: cbergson{at}mail.mcg.edu.

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