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Published online
doi:10.1083/jcb.200902146
The Journal of Cell Biology, Vol. 186, No. 3, 343-353
The Rockefeller University Press, 0021-9525 $30.00
© Xu et al.
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A role of histone H3 lysine 4 methyltransferase components in endosomal trafficking



Zhuojin Xu1,2, Qiang Gong1,2, Bin Xia1,3, Benjamin Groves1,2, Marc Zimmermann1, Chris Mugler1, Dezhi Mu3, Brian Matsumoto2, Matthew Seaman4,5, and Dzwokai Ma1,2

1 Department of Molecular, Cellular, and Developmental Biology and 2 Neuroscience Research Institute, University of California, Santa Barbara, Santa Barbara, CA 93106
3 Department of Pediatrics, West China Second Hospital, Sichuan University, Chengdu, Sichuan Province, China 610041
4 Cambridge Institute for Medical Research and 5 Department of Clinical Biochemistry, University of Cambridge, Cambridge, England CB2 0XY, UK

Correspondence to Dzwokai Ma: ma{at}lifesci.ucsb.edu

Histone lysine methyltransferase complexes are essential for chromatin organization and gene regulation. Whether any of this machinery functions in membrane traffic is unknown. In this study, we report that mammal Dpy-30 (mDpy-30), a subunit of several histone H3 lysine 4 (H3K4) methyltransferase (H3K4MT) complexes, resides in the nucleus and at the trans-Golgi network (TGN). The TGN targeting of mDpy-30 is mediated by BIG1, a TGN-localized guanine nucleotide exchange factor for adenosine diphosphate ribosylation factor GTPases. Altering mDpy-30 levels changes the distribution of cation-independent mannose 6-phosphate receptor (CIMPR) without affecting that of TGN46 or transferrin receptor. Our experiments also indicate that mDpy-30 functions in the endosome to TGN transport of CIMPR and that its knockdown results in the enrichment of internalized CIMPR and recycling endosomes near cell protrusions. Much like mDpy-30 depletion, the knockdown of Ash2L or RbBP5, two other H3K4MT subunits, leads to a similar redistribution of CIMPR. Collectively, these results suggest that mDpy-30 and probably H3K4MT play a role in the endosomal transport of specific cargo proteins.

© 2009 Xu et al.
This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

Z. Xu, Q. Gong, and B. Xia contributed equally to this paper.

Abbreviations used in this paper: CIMPR, cation-independent mannose 6-phosphate receptor; Flp, flippase recombination enzyme; mDpy-30, mammal Dpy-30; PM, plasma membrane; TfnR, transferrin receptor.


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