On the Detection and Functional Significance of the Protein–Protein 
Interactions of Mitochondrial Transport Proteins

Zhang, YJ; Fernie, A. R.

doi:10.3390/biom10081107

Datensatz

DATENSATZ AKTIONENEXPORT

Zur Ablage hinzufügen

Lokale TagsFreigabegeschichteDetailsÜbersicht

Freigegeben

Zeitschriftenartikel

On the Detection and Functional Significance of the Protein–Protein Interactions of Mitochondrial Transport Proteins

MPG-Autoren

/persons/resource/persons135687

Zhang, YJ
Central Metabolism, Department Willmitzer, Max Planck Institute of Molecular Plant Physiology, Max Planck Society;

/persons/resource/persons97147

Fernie, A. R.
Central Metabolism, Department Willmitzer, Max Planck Institute of Molecular Plant Physiology, Max Planck Society;

Externe Ressourcen

Link
(beliebiger Volltext)

Volltexte (beschränkter Zugriff)

Für Ihren IP-Bereich sind aktuell keine Volltexte freigegeben.

Volltexte (frei zugänglich)

Es sind keine frei zugänglichen Volltexte in PuRe verfügbar

Ergänzendes Material (frei zugänglich)

Es sind keine frei zugänglichen Ergänzenden Materialien verfügbar

Zitation

Zhang, Y., & Fernie, A. R. (2020). On the Detection and Functional Significance of the Protein–Protein Interactions of Mitochondrial Transport Proteins. Biomolecules, 10(8): 1107. doi:10.3390/biom10081107.

Zitierlink: https://hdl.handle.net/21.11116/0000-0006-CD02-1

Zusammenfassung

Proteinndash;protein assemblies are highly prevalent in all living cells. Considerable evidence has recently accumulated suggesting that particularly transient association/dissociation of proteins represent an important means of regulation of metabolism. This is true not only in the cytosol and organelle matrices, but also at membrane surfaces where, for example, receptor complexes, as well as those of key metabolic pathways, are common. Transporters also frequently come up in lists of interacting proteins, for example, binding proteins that catalyze the production of their substrates or that act as relays within signal transduction cascades. In this review, we provide an update of technologies that are used in the study of such interactions with mitochondrial transport proteins, highlighting the difficulties that arise in their use for membrane proteins and discussing our current understanding of the biological function of such interactions.