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Details on Person YME1L1 (YME1L, i-AAA) is a homohexameric zinc metalloproteas...
| Class:Id | Summation:9839791 |
|---|---|
| _displayName | YME1L1 (YME1L, i-AAA) is a homohexameric zinc metalloproteas... |
| _timestamp | 2023-11-06 05:36:25 |
| 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: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:9852591] May, Bruce, 2023-11-06 |
| text | YME1L1 (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 processively unfolded and translocated in an ATP-dependent reaction to a central pore formed by the protease domains of the YME1L1 complex. 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) | [Reaction:9839772] YME1L1 binds mitochondrial intermembrane space proteins [Homo sapiens] |
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