MPP cleaves targeting peptide (presequence) of matrix precursors

Stable Identifier
R-HSA-1299478
Type
Reaction [transition]
Species
Homo sapiens
Compartment
mitochondrial inner membrane
ReviewStatus
5/5
Locations in the PathwayBrowser
Expand all
General
SVG | 
PNG
Low
Medium
High
 | PPTX  | SBGN
MPP cleaves targeting peptide (presequence) of matrix precursors
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

As inferred from yeast, the alpha subunit of the mitochondrial processing peptidase (MPP) binds presequences of mitochondrial precursors and the beta subunit cleaves the presequence. After cleavage, proteins destined for the matrix are drawn into the matrix by ATP-dependent interaction with mtHSP70 (HSPA9, homolog of yeast SSC1) of the PAM complex.

Literature References
PubMed ID Title Journal Year
19453276 Multiple pathways for mitochondrial protein traffic

Yamano, K, Endo, T

Biol Chem 2009
18174896 Multiple pathways for sorting mitochondrial precursor proteins

Pfanner, N, Wagner, R, Sickmann, A, Bolender, N, Meisinger, C

EMBO Rep 2008
Participants
Input
Output
Participates
as an event of
Catalyst Activity

metalloendopeptidase activity of Mitochondrial processing peptidase [mitochondrial inner membrane]

Physical Entity
Mitochondrial processing peptidase [mitochondrial inner membrane] (Homo sapiens)
Activity
metalloendopeptidase activity (GO:0004222)
Inferred From
MPP hydrolyzes presequence of matrix precursors (Saccharomyces cerevisiae)
Authored
May, B  (2011-05-21)
Reviewed
Endo, T  (2012-02-12)
D'Eustachio, P  (2011-11-02)
Created
May, B  (2011-05-23)
Cite Us!