Reaction participants Show >> << Hide
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Namehelp_outline
[protein]-C-terminal L-amino acid-glycyl-phosphatidylserine
Identifier
RHEA-COMP:17326
Reactive part
help_outline
- Name help_outline C-terminal L-amino acid-(phosphatidylserine)-amidated glycine residue Identifier CHEBI:172942 Charge -2 Formula C12H14N3O12PR3 SMILEShelp_outline O(P(=O)(OC[C@@H](C([O-])=O)NC(CNC(=O)[C@@H](N*)*)=O)[O-])C[C@H](OC(*)=O)COC(*)=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,648 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 1,2-diacyl-sn-glycero-3-phospho-L-serine-N-glycine Identifier CHEBI:176543 Charge -1 Formula C10H14N2O11PR2 SMILEShelp_outline P([O-])(=O)(OC[C@@H](C(=O)[O-])NC(C[NH3+])=O)OC[C@@H](COC(=O)*)OC(=O)* 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
[protein]-C-terminal L-amino acid
Identifier
RHEA-COMP:17349
Reactive part
help_outline
- Name help_outline C-terminal proteinogenic amino-acid residue Identifier CHEBI:90782 Charge -1 Formula C2H2NO2R SMILEShelp_outline N([C@H](C([O-])=O)*)* 2D coordinates Mol file for the small molecule Search links Involved in 17 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:67912 | RHEA:67913 | RHEA:67914 | RHEA:67915 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Delipidation of mammalian Atg8-family proteins by each of the four ATG4 proteases.
Kauffman K.J., Yu S., Jin J., Mugo B., Nguyen N., O'Brien A., Nag S., Lystad A.H., Melia T.J.
During macroautophagy/autophagy, mammalian Atg8-family proteins undergo 2 proteolytic processing events. The first exposes a COOH-terminal glycine used in the conjugation of these proteins to lipids on the phagophore, the precursor to the autophagosome, whereas the second releases the lipid. The A ... >> More
During macroautophagy/autophagy, mammalian Atg8-family proteins undergo 2 proteolytic processing events. The first exposes a COOH-terminal glycine used in the conjugation of these proteins to lipids on the phagophore, the precursor to the autophagosome, whereas the second releases the lipid. The ATG4 family of proteases drives both cleavages, but how ATG4 proteins distinguish between soluble and lipid-anchored Atg8 proteins is not well understood. In a fully reconstituted delipidation assay, we establish that the physical anchoring of mammalian Atg8-family proteins in the membrane dramatically shifts the way ATG4 proteases recognize these substrates. Thus, while ATG4B is orders of magnitude faster at processing a soluble unprimed protein, all 4 ATG4 proteases can be activated to similar enzymatic activities on lipid-attached substrates. The recognition of lipidated but not soluble substrates is sensitive to a COOH-terminal LIR motif both in vitro and in cells. We suggest a model whereby ATG4B drives very fast priming of mammalian Atg8 proteins, whereas delipidation is inherently slow and regulated by all ATG4 homologs. << Less
Autophagy 14:992-1010(2018) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.