NDLI: Autocatalytic Processing of m-AAA Protease Subunits in Mitochondria

Content Provider	PubMed Central
Author	Koppen, Mirko Bonn, Florian Sarah, Ehses Langer, Thomas
Editor	Shaw, Janet M.
Abstract	m-AAA proteases are ATP-dependent proteolytic machines in the inner membrane of mitochondria which are crucial for the maintenance of mitochondrial activities. Conserved nuclear-encoded subunits, termed paraplegin, Afg3l1, and Afg3l2, form various isoenzymes differing in their subunit composition in mammalian mitochondria. Mutations in different m-AAA protease subunits are associated with distinct neuronal disorders in human. However, the biogenesis of m-AAA protease complexes or of individual subunits is only poorly understood. Here, we have examined the processing of nuclear-encoded m-AAA protease subunits upon import into mitochondria and demonstrate autocatalytic processing of Afg3l1 and Afg3l2. The mitochondrial processing peptidase MPP generates an intermediate form of Afg3l2 that is matured autocatalytically. Afg3l1 or Afg3l2 are also required for maturation of newly imported paraplegin subunits after their cleavage by MPP. Our results establish that mammalian m-AAA proteases can act as processing enzymes in vivo and reveal overlapping activities of Afg3l1 and Afg3l2. These findings might be of relevance for the pathogenesis of neurodegenerative disorders associated with mutations in different m-AAA protease subunits.
Related Links	http://dx.doi.org/10.1091/mbc.e09-03-0218
Ending Page	4224
Page Count	9
Starting Page	4216
File Format	PDF
ISSN	10591524
e-ISSN	19394586
Journal	Molecular Biology of the Cell
Issue Number	19
Volume Number	20
Language	English
Publisher	The American Society for Cell Biology
Publisher Date	2009-10-01
Access Restriction	Open
Rights Holder	The American Society for Cell Biology
Subject Keyword	Cell Biology Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Molecular Biology

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