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A role of histone H3 lysine 4 methyltransferase components in endosomal trafficking

Zhuojin Xu1, Qiang Gong, Bin Xia

  • 1Department of Molecular, Cellular, and Developmental Biology, University of California, Santa Barbara, Santa Barbara, CA 93106, USA.

The Journal of Cell Biology
|August 5, 2009
PubMed

Insights

Mammal Dpy-30 (mDpy-30), a histone methyltransferase subunit, functions in the trans-Golgi network and endosomal transport. This suggests histone H3 lysine 4 methyltransferase complexes play a role in membrane traffic.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Epigenetics

Background:

  • Histone lysine methyltransferase complexes regulate chromatin organization and gene expression.
  • The role of these complexes in membrane trafficking pathways remains unexplored.

Purpose of the Study:

  • To investigate the potential function of histone methyltransferase machinery in membrane traffic.
  • To determine the localization and function of mammal Dpy-30 (mDpy-30) in cellular transport pathways.

Main Methods:

  • Immunofluorescence microscopy to determine protein localization.
  • Analysis of receptor distribution upon alteration of mDpy-30 levels.
  • Knockdown experiments to assess the functional impact of mDpy-30, Ash2L, and RbBP5.

Main Results:

  • Mammal Dpy-30 localizes to both the nucleus and the trans-Golgi network (TGN), with TGN targeting mediated by BIG1.
  • Altering mDpy-30 levels affects the distribution of cation-independent mannose 6-phosphate receptor (CIMPR) but not TGN46 or transferrin receptor.
  • mDpy-30 knockdown impairs endosome-to-TGN transport of CIMPR, leading to its accumulation in recycling endosomes.
  • Knockdown of other H3K4MT subunits (Ash2L, RbBP5) similarly affects CIMPR distribution.

Conclusions:

  • Mammal Dpy-30 is involved in the endosomal transport of specific cargo proteins, notably CIMPR.
  • The study reveals a novel role for histone H3 lysine 4 methyltransferase (H3K4MT) complexes in membrane trafficking pathways.
  • These findings suggest a link between epigenetic regulatory machinery and cellular membrane dynamics.

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