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Details on Person YME1L1 (YME1L, i-AAA+) is a homohexameric zinc metalloprotea...

Class:IdSummation:9839790
_displayNameYME1L1 (YME1L, i-AAA+) is a homohexameric zinc metalloprotea...
_timestamp2023-11-06 05:36:30
created[InstanceEdit:9839776] May, Bruce, 2023-07-10
literatureReference[LiteratureReference:9839114] Impaired folding of the mitochondrial small TIM chaperones induces clearance by the i-AAA protease
[LiteratureReference:9839132] Multiple genes, including a member of the AAA family, are essential for degradation of unassembled subunit 2 of cytochrome c oxidase in yeast mitochondria
[LiteratureReference:9839775] Identification and characterization of YME1L1, a novel paraplegin-related gene
[LiteratureReference:9839797] The human homologue of the yeast mitochondrial AAA metalloprotease Yme1p complements a yeast yme1 disruptant
[LiteratureReference:8953742] The membrane scaffold SLP2 anchors a proteolytic hub in mitochondria containing PARL and the i-AAA protease YME1L
[LiteratureReference:9839839] Substrate recognition by AAA+ ATPases: distinct substrate binding modes in ATP-dependent protease Yme1 of the mitochondrial intermembrane space
modified[InstanceEdit:9839857] May, Bruce, 2023-07-10
[InstanceEdit:9840221] May, Bruce, 2023-07-14
[InstanceEdit:9852591] May, Bruce, 2023-11-06
textYME1L1 (YME1L, i-AAA+) is a homohexameric zinc metalloprotease that is anchored in the inner membrane and protrudes into the mitochondrial intermembrane space (Coppola et al. 2000, Shah et al. 2000, Wai et al. 2016). Substrate proteins of YME1L1 initially bind conserved helices at the N-terminal end of the ATPase domain and at the C-terminal domain of the protease domain (inferred from the yeast homolog in Graef et al. 2007). The substrate protein is unfolded and translocated processively in an ATP-dependent reaction to a central pore formed by the protease domains of the YME1L1 complex.
YME1L1 binds, unfolds, and degrades specific inner membrane proteins (MacVicar et al. 2019). These include components of the mitochondrial import apparatus: TIMM17A (Rainbolt et al. 2013), TIMM22 (MacVicar et al. 2019), and improperly folded TIMM9 and TIMM10 (inferred from yeast homologs in Baker et al. 2012). Substrates of YME1L1 also include components of the respiratory chain: MT‑ND1 and MT‑CO4 (Stiburek et al. 2012, Cesnekova et al. 2018), unassembled MT‑CO2 (inferred from yeast homologs in Nakai et al. 1995), and subunits of respiratory chain complex I (Cesnekova et al. 2018) such as unassembled NDUFB6 (Stiburek et al. 2012, Cesnekova et al. 2018). YME1L1 also degrades the protease OMA1 (Rainbolt et al. 2016), a stress-activated ATP-independent protease that can act reciprocally to YME1L1, and OPA1 (Cesnekova et al. 2018), a dynamin-like protein that controls mitochondrial morphology.
(summation)[Reaction:9839064] YME1L1 binds mitochondrial inner membrane proteins [Homo sapiens]
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