ABCD2 identifies a subclass of peroxisomes in mouse adipose tissue

Xiaoxi Liu, Jingjing Liu, Joshua D. Lester, Sonja S. Pijut, Gregory A. Graf

Research output: Contribution to journalArticlepeer-review

8 Scopus citations


ATP-binding cassette transporter D2 (D2) is an ABC half transporter that is thought to promote the transport of very long-chain fatty acyl-CoAs into peroxisomes. Both D2 and peroxisomes increase during adipogenesis. Although peroxisomes are essential to both catabolic and anabolic lipid metabolism, their function, and that of D2, in adipose tissues remain largely unknown. Here, we investigated the D2 localization and the proteome of D2-containing organelles, in adipose tissue. Centrifugation of mouse adipose homogenates generated a fraction enriched with D2, but deficient in peroxisome markers including catalase, PEX19, and ABCD3 (D3). Electron microscopic imaging of this fraction confirmed the presence of D2 protein on an organelle with a dense matrix and a diameter of ∼200 nm, the typical structure and size of a microperoxisome. D2 and PEX19 antibodies recognized distinct structures in mouse adipose. Immunoisolation of the D2-containing compartment confirmed the scarcity of PEX19 and proteomic profiling revealed the presence of proteins associated with peroxisome, endoplasmic reticulum (ER), and mitochondria. D2 is localized to a distinct class of peroxisomes that lack many peroxisome proteins, and may associate physically with mitochondria and the ER.

Original languageEnglish
Pages (from-to)129-134
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number1
StatePublished - Jan 2 2015

Bibliographical note

Publisher Copyright:
© 2014 Elsevier Inc. All rights reserved.


  • ABC transporter
  • Adipose tissue
  • Peroxisome
  • Proteomics
  • Subcellular organelle

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


Dive into the research topics of 'ABCD2 identifies a subclass of peroxisomes in mouse adipose tissue'. Together they form a unique fingerprint.

Cite this