Journal of Inherited Metabolic Disease

, Volume 32, Issue 2, pp 163–180

Organelle dynamics and dysfunction: A closer link between peroxisomes and mitochondria

Authors

  • F. Camões
    • Centre for Cell Biology & Department of BiologyUniversity of Aveiro
  • N. A. Bonekamp
    • Centre for Cell Biology & Department of BiologyUniversity of Aveiro
  • H. K. Delille
    • Centre for Cell Biology & Department of BiologyUniversity of Aveiro
    • Centre for Cell Biology & Department of BiologyUniversity of Aveiro
SSIEM Symposium 2008

DOI: 10.1007/s10545-008-1018-3

Cite this article as:
Camões, F., Bonekamp, N.A., Delille, H.K. et al. J Inherit Metab Dis (2009) 32: 163. doi:10.1007/s10545-008-1018-3

Summary

Mitochondria and peroxisomes are ubiquitous subcellular organelles, which fulfil an indispensable role in the cellular metabolism of higher eukaryotes. Moreover, they are highly dynamic and display large plasticity. There is growing evidence now that both organelles exhibit a closer interrelationship than previously appreciated. This connection includes metabolic cooperations and cross-talk, a novel putative mitochondria-to-peroxisome vesicular trafficking pathway, as well as an overlap in key components of their fission machinery. Thus, peroxisomal alterations in metabolism, biogenesis, dynamics and proliferation can potentially influence mitochondrial functions, and vice versa. In this review, we present the latest progress in the emerging field of peroxisomal and mitochondrial interrelationship with a particular emphasis on organelle dynamics and its implication in diseases.

Abbreviations

DLP

dynamin-like protein

ER

endoplasmic reticulum

MDV

mitochondria-derived vesicle

MIM

mitochondrial inner membrane

MOM

mitochondrial outer membrane

MOMP

mitochondrial outer membrane permeabilization

mtDNA

mitochondrial DNA

PBD

peroxisome biogenesis disorder

PEX

peroxin

PMP

peroxisomal membrane protein

PTS

peroxisomal targeting signal

ROS

reactive oxygen species

SUMO

small ubiquitin-like modifier

TA

tail-anchored

TMD

transmembrane domain

VLCFA

very long-chain fatty acids

Copyright information

© Springer Science+Business Media B.V. 2008