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J. Biol. Chem., Vol. 283, Issue 25, 17092-17098, June 20, 2008

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Lipid-independent Secretion of a Drosophila Wnt Protein^*

Wendy Ching, Howard C. Hang¹, and Roel Nusse²

From the Howard Hughes Medical Institute and the Department of Developmental Biology, Stanford University School of Medicine, Stanford, California 94305 and the Laboratory of Chemical Biology and Microbial Pathogenesis, The Rockefeller University, New York, New York 10065

Wnt proteins comprise a large class of secreted signaling molecules with key roles during embryonic development and throughout adult life. Recently, much effort has been focused on understanding the factors that regulate Wnt signal production. For example, Porcupine and Wntless/Evi/Sprinter have been identified as being required in Wnt-producing cells for the processing and secretion of many Wnt proteins. Interestingly, in this study we find that WntD, a recently characterized Drosophila Wnt family member, does not require Porcupine or Wntless/Evi/Sprinter for its secretion or signaling activity. Because Porcupine is involved in post-translational lipid modification of Wnt proteins, we used a novel labeling method and mass spectrometry to ask whether WntD undergoes lipid modification and found that it does not. Although lipid modification is also hypothesized to be required for Wnt secretion, we find that WntD is secreted very efficiently. WntD secretion does, however, maintain a requirement for the secretory pathway component Rab1. Our results show that not all Wnt family members require lipid modification, Porcupine, or Wntless/Evi/Sprinter for secretion and suggest that different modes of secretion may exist for different Wnt proteins.

Received for publication, March 14, 2008 , and in revised form, April 21, 2008.

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^* This work was supported in part by the Howard Hughes Medical Institute (to W. C. and R. N.) and the National Science Foundation (to W. C.). 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 Supported by The Rockefeller University and The Irma T. Hirschl Trust.

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² To whom correspondence should be addressed. E-mail: rnusse{at}stanford.edu.

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