The Tightly Regulated and Compartmentalised Import, Sorting and Folding of Mitochondrial Proteins
Laura Cassina, Giorgio Casari*
Identifiers and Pagination:Year: 2009
First Page: 200
Last Page: 221
Publisher Id: TOBIOJ-2-200
Article History:Received Date: 06/05/2009
Revision Received Date: 29/07/2009
Acceptance Date: 12/08/2009
Electronic publication date: 31/12/2009
Collection year: 2009
open-access license: This is an open access article distributed under the terms of the Creative Commons Attribution 4.0 International Public License (CC-BY 4.0), a copy of which is available at: (https://creativecommons.org/licenses/by/4.0/legalcode). This license permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Mitochondria are eukaryotic intracellular organelles that still bear the signatures of their prokaryotic ancestor and require nuclear assistance. They generously dispense energy to cells, but are also involved in several biosynthetic processes, as well as in cell signalling pathways and programmed cell death.
Mitochondria are partitioned into four intra-organelle compartments: the outer membrane, the inner membrane, the intermembrane space and the matrix. Each compartment contains a unique set of proteins and a personalised system for guaranteeing protein homeostasis.
What follows is a survey of the function and topology of the multiple systems that operate the concerted action of protein sorting and folding in the four mitochondrial compartments.