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

Class:IdSummation:9839800
_displayNameYME1L1 (YME1L, i-AAA) is a hexameric metalloprotease that is...
_timestamp2023-11-06 05:36:21
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
modified[InstanceEdit:9839857] May, Bruce, 2023-07-10
[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, 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 intermembrane space proteins, including STARD7 (Saita et al. 2018, MacVicar et al. 2019), TRIAP1 (MacVicar et al. 2019), PRELID1 (Potting et al. 2013, MacVicar et al. 2019), and CHCHD2 (also called MNRR) (Aras et al. 2020).
(summation)[BlackBoxEvent:9839751] YME1L1 degrades mitochondrial intermembrane space proteins [Homo sapiens]
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