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Details on Person YME1L1 (YME1L, i-AAA) is a hexameric metalloprotease that is...

Class:IdSummation:9839799
_displayNameYME1L1 (YME1L, i-AAA) is a hexameric metalloprotease that is...
_timestamp2023-11-06 05:36:17
created[InstanceEdit:9839776] May, Bruce, 2023-07-10
literatureReference[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:9839842] Structure of the mitochondrial inner membrane AAA+ protease YME1 gives insight into substrate processing
[LiteratureReference:9839114] Impaired folding of the mitochondrial small TIM chaperones induces clearance by the i-AAA protease
modified[InstanceEdit:9839857] May, Bruce, 2023-07-10
[InstanceEdit:9840708] May, Bruce, 2023-07-25
[InstanceEdit:9852591] May, Bruce, 2023-11-06
textYME1L1 (YME1L, i-AAA) is a hexameric 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). Each monomer of YME1L1 contains a membrane-proximal ATPase and protein unfolding domain and a membrane-distal protease domain (inferred from the yeast homolog in Puchades et al. 2017). The substrate protein enters a central channel formed by the ATPase domains, where it is unfolded and translocated into the pore formed by the protease domains (inferred from the yeast homolog in Puchades et al. 2017). Within the protease pore, it is hydrolyzed by zinc cofactors bound to the protease domains (inferred from the yeast homolog in Puchades et al. 2017).
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)[BlackBoxEvent:9839146] YME1L1 degrades mitochondrial inner membrane proteins [Homo sapiens]
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