Literature DB >> 25109985

Mechanisms and physiological impact of the dual localization of mitochondrial intermembrane space proteins.

Carmelina Petrungaro1, Jan Riemer1.   

Abstract

Eukaryotic cells developed diverse mechanisms to guide proteins to more than one destination within the cell. Recently, the proteome of the IMS (intermembrane space) of mitochondria of yeast cells was identified showing that approximately 20% of all soluble IMS proteins are dually localized to the IMS, as well as to other cellular compartments. Half of these dually localized proteins are important for oxidative stress defence and the other half are involved in energy homoeostasis. In the present review, we discuss the mechanisms leading to the dual localization of IMS proteins and the implications for mitochondrial function.

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Year:  2014        PMID: 25109985     DOI: 10.1042/BST20140104

Source DB:  PubMed          Journal:  Biochem Soc Trans        ISSN: 0300-5127            Impact factor:   5.407


  3 in total

1.  The ARL2 GTPase regulates mitochondrial fusion from the intermembrane space.

Authors:  Laura E Newman; Cara R Schiavon; Rachel E Turn; Richard A Kahn
Journal:  Cell Logist       Date:  2017-06-23

Review 2.  Cytosolic redox components regulate protein homeostasis via additional localisation in the mitochondrial intermembrane space.

Authors:  Mauricio Cardenas-Rodriguez; Kostas Tokatlidis
Journal:  FEBS Lett       Date:  2017-08-06       Impact factor: 4.124

Review 3.  The mitochondrial intermembrane space: the most constricted mitochondrial sub-compartment with the largest variety of protein import pathways.

Authors:  Ruairidh Edwards; Ross Eaglesfield; Kostas Tokatlidis
Journal:  Open Biol       Date:  2021-03-10       Impact factor: 6.411

  3 in total

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