Multiple pathways for sorting mitochondrial precursor proteins

Autor(en): Bolender, Natalia
Sickmann, Albert
Wagner, Richard 
Meisinger, Chris
Pfanner, Nikolaus
Stichwörter: ADP/ATP CARRIER; ASSEMBLY PATHWAY; Biochemistry & Molecular Biology; BIOGENESIS; Cell Biology; COMPLEX; IMPORT MOTOR; INNER MEMBRANE; INTERMEMBRANE SPACE PROTEINS; MIA; OUTER-MEMBRANE; PAM; PREPROTEIN TRANSLOCASE; PRESEQUENCE TRANSLOCASE; SAM; TIM; TOM
Erscheinungsdatum: 2008
Herausgeber: NATURE PUBLISHING GROUP
Enthalten in: EMBO REPORTS
Band: 9
Ausgabe: 1
Startseite: 42
Seitenende: 49
Zusammenfassung: 
Mitochondria import hundreds of different precursor proteins from the cytosol. More than 50% of mitochondrial proteins do not use the classical import pathway that is guided by amino-terminal pre-sequences, but instead contain different types of internal targeting signals. Recent studies have revealed an unexpected complexity of the mitochondrial protein import machinery and have led to the discovery of new transport pathways. Here, we review the versatility of mitochondrial protein import and its connection to mitochondrial morphology, redox regulation and energetics.
ISSN: 1469221X
DOI: 10.1038/sj.embor.7401126

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