Autophagin

Autophagin-1 (Atg4/Apg4) is a unique cysteine protease responsible for the cleavage of the carboxyl terminus of Atg8/Apg8/Aut7, a reaction essential for its lipidation during autophagy. Human Atg4 homologues cleave the carboxyl termini of the three human Atg8 homologues, microtubule-associated protein light chain 3 (LC3), GABARAP, and GATE-16. The Protein is approximately 393 amino acids long and has a relative molecular mass of about 43-44 kDa.

Autophagy is currently being researched in relation to several human disorders. The future challenge is to develop methods to separately manipulate the activity of each of the autophagic pathways. This would allow researchers to further understand their contribution to disease such as cancer, neurodegeneration, infectious disease, muscular disorders and possibly will provide therapeutic tools.

See also

References

  1. ↑ Development by self-digestion: molecular mechanisms and biological functions of autophagy by Levine B, Klionsky DJ. in Dev Cell. 2004 Apr;6(4):463-77. Review.
  2. ↑ HsAtg4B/HsApg4B/autophagin-1 cleaves the carboxyl termini of three human Atg8 homologues and delipidates microtubule-associated protein light chain 3- and GABAA receptor-associated protein-phospholipid conjugates byTanida I, Sou YS, Ezaki J, Minematsu-Ikeguchi N, Ueno T, Kominami E. in J Biol Chem. 2004 Aug 27;279(35):36268-76
  3. ↑ "UniProt". UniProt. Retrieved 2026-09-04.
  4. ↑ Maruyama, Tatsuro; Noda, Nobuo N. (January 2018). "Autophagy-regulating protease Atg4: structure, function, regulation and inhibition". The Journal of Antibiotics. 71 (1). Nature Publishing Group: 72–78. doi:10.1038/ja.2017.104. ISSN 1881-1469. PMC 5799747. PMID 28901328.
  5. ↑ "ATG4B (human recombinant)". www.caymanchem.com. Retrieved 2026-09-04.
  6. ↑ Autophagy: in sickness and in health by Cuervo AM. in Trends Cell Biol. 2004 Feb;14(2):70-7.