3.4.24.B19: i-AAA protease
This is an abbreviated version!
For detailed information about i-AAA protease, go to the full flat file.
Word Map on EC 3.4.24.B19
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3.4.24.B19
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intermembrane
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xiap
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survivin
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proteostasis
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dynamin-like
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degradation
- 3.4.24.B19
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intermembrane
- xiap
- survivin
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proteostasis
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dynamin-like
- degradation
Reaction
proteolytic degradation of proteins =
Synonyms
AAA protease, casein lytic proteinase XP, ClpXP, FtsH4, i-AAA Protease, IAP, IAP-1, M41.004, OSD1 protein, TAT-binding homolog 11, YME1, YME1 AAA protease, Yme1L, Yme1p
ECTree
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General Information
General Information on EC 3.4.24.B19 - i-AAA protease
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malfunction
metabolism
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constitutive OPA1 cleavage by YME1L and OMA1 at two distinct sites leads to the accumulation of both long and short forms of OPA1 and maintains mitochondrial fusion
physiological function
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a IAP deletion strain is neither impaired in viability, nor does it show any changes in morphology under standard growth conditions (20°C) but shows increased lifespan and is sensitive to elevated temperature (37°C). Deletion of IAP affects the composition of the mitochondrial respiratory chain complexes
malfunction
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mutations in the catalytic subunit of the i-AAA protease complex cause an elevated rate of mitochondrial turnover. Inactivation of the enzyme results in a slight increase in H2O2 sensitivity; while inactivation of both TAZ1 and YME1 together results in a dramatic increase in H2O2 sensitivity
malfunction
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mutations in the catalytic subunit of the i-AAA protease complex cause an elevated rate of mitochondrial turnover. Inactivation of the enzyme results in a slight increase in H2O2 sensitivity; while inactivation of both TAZ1 and YME1 together results in a dramatic increase in H2O2 sensitivity
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stress-induced YME1L degradation attenuates protective regulation of mitochondrial proteostasis and promotes cellular death in response to oxidative stress
physiological function
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the mitochondrial i-AAA protease Yme1 mediates Atg32 processing and is required for mitophagy. The enzyme regulates the Atg32-Atg11 interaction
physiological function
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the protease Yme1 is required for efficient mitophagy in the absence of tafazzin. The catalytic subunit of the i-AAA protease complex is responsible for degradation of unfolded or misfolded mitochondrial gene products and also has a role in intermembrane space protein folding
physiological function
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Yme1 has a folding assistant function for dihydrofolate reductase in the intermembrane space, in addition to its proteolytic function, in the protein homeostasis of mitochondria
physiological function
abundance of the Tim17-2 protein, an essential component of the TIM17:23 translocase, is directly controlled by the proteolytic activity of FTSH4. Plants that are lacking functional FTSH4 protease display a significantly enhanced capacity of preprotein import through the TIM17:23-dependent pathway
physiological function
both m-AAA and i-AAA complexes coordinately regulate OMA1 processing and turnover, and consequently control which OPA1 isoforms are present
physiological function
mice lacking YME1L in the nervous system manifest ocular dysfunction with microphthalmia and cataracts and develop deficiencies in locomotor activity due to specific degeneration of spinal cord axons. Mitochondrial fragmentation occurs throughout the nervous system and does not correlate with the degenerative phenotype. Deletion of metalloprotease Oma1 restores tubular mitochondria but deteriorates axonal degeneration in the absence of YME1L
physiological function
YME1L-deficient mice manifest ocular dysfunction with microphthalmia and cataracts and develop deficiencies in locomotor activity due to specific degeneration of spinal cord axons, which relay proprioceptive signals from the hind limbs to the cerebellum. Mitochondrial fragmentation occurs throughout the nervous system and does not correlate with the degenerative phenotype. Deletion of metalloendopeptidase Oma1 restores tubular mitochondria but deteriorates axonal degeneration in the absence of YME1L
physiological function
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the protease Yme1 is required for efficient mitophagy in the absence of tafazzin. The catalytic subunit of the i-AAA protease complex is responsible for degradation of unfolded or misfolded mitochondrial gene products and also has a role in intermembrane space protein folding
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physiological function
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abundance of the Tim17-2 protein, an essential component of the TIM17:23 translocase, is directly controlled by the proteolytic activity of FTSH4. Plants that are lacking functional FTSH4 protease display a significantly enhanced capacity of preprotein import through the TIM17:23-dependent pathway
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