YME1 degrades TIM10

Stable Identifier
R-SCE-9839836
Type
Reaction [omitted]
Species
Saccharomyces cerevisiae
Compartment
mitochondrial inner membrane
ReviewStatus
5/5
General
SVG | 
PNG
Low
Medium
High
 | PPTX  | SBGN
YME1 degrades TIM10
Each monomer of YME1L1 contains a membrane proximal ATPase, protein unfolding domain and a membrane distal protease domain (Leonhard et al. 1996, Puchades et al. 2017). The substrate protein enters a central channel formed by the ATPase domains, where it is processively unfolded and translocated into the pore formed by the protease domains (Puchades et al. 2017). Within the protease pore, it is hydrolyzed by zinc cofactors bound to the protease domains (Puchades et al. 2017).
Literature References
PubMed ID Title Journal Year
8861950 AAA proteases with catalytic sites on opposite membrane surfaces comprise a proteolytic system for the ATP-dependent degradation of inner membrane proteins in mitochondria

Leonhard, K, Herrmann, JM, Stuart, RA, Mannhaupt, G, Neupert, W, Langer, T

EMBO J 1996
29097521 Structure of the mitochondrial inner membrane AAA+ protease YME1 gives insight into substrate processing

Puchades, C, Rampello, AJ, Shin, M, Giuliano, CJ, Wiseman, RL, Glynn, SE, Lander, GC

Science 2017
Participants
Input
Output
Orthologous Events
YME1L1 degrades mitochondrial inner membrane proteins (Homo sapiens)
YME1L1 degrades mitochondrial intermembrane space proteins (Homo sapiens)
Authored
May, B  (2023-07-10)
Reviewed
Aljghami, ME  (2023-11-04)
Houry, WA  (2023-11-04)
Morey, T  (2023-11-04)
Created
May, B  (2023-07-10)
Cite Us!