5jhc

Structural highlights

Function

AMPL_YEAST Resident vacuolar enzyme that catalyzes the removal of amino acids from the N-terminus of peptides and proteins. Also acts as the major cargo protein of the cytoplasm-to-vacuole targeting (Cvt) pathway. The precursor form of aminopeptidase 1 (prApe1) assembles into dodecamers and the propeptide mediates the aggregation of dodecamers into higher multimers. The multimers are then recognized via the propeptide by their receptor ATG19, and ATG19 further interacts with ATG11, which tethers the APE1-ATG19 complex to the pre-autophagosomal structure (PAS). The cargo-receptor complex (also Cvt complex) is selectively enwrapped by a double-membrane structure termed the Cvt vesicle under vegetative growth conditions and by a similar but larger double-membrane structure termed the autophagosome under nitrogen starvation conditions. The Cvt vesicle or the autophagosome fuses with the vacuolar membrane and release its content in the vacuolar lumen. In the vacuole, prApe1 is processed into mature aminopeptidase 1 (mApe1).^{[1] [2] [3] [4] [5] [6] [7] [8]}

See Also

• Aminopeptidase 3D structures

References

1. ↑ Leber R, Silles E, Sandoval IV, Mazon MJ. Yol082p, a novel CVT protein involved in the selective targeting of aminopeptidase I to the yeast vacuole. J Biol Chem. 2001 Aug 3;276(31):29210-7. Epub 2001 May 29. PMID:11382752 doi:http://dx.doi.org/10.1074/jbc.M101438200
2. ↑ Scott SV, Guan J, Hutchins MU, Kim J, Klionsky DJ. Cvt19 is a receptor for the cytoplasm-to-vacuole targeting pathway. Mol Cell. 2001 Jun;7(6):1131-41. PMID:11430817
3. ↑ Shintani T, Klionsky DJ. Cargo proteins facilitate the formation of transport vesicles in the cytoplasm to vacuole targeting pathway. J Biol Chem. 2004 Jul 16;279(29):29889-94. Epub 2004 May 11. PMID:15138258 doi:http://dx.doi.org/10.1074/jbc.M404399200
4. ↑ Morales Quinones M, Winston JT, Stromhaug PE. Propeptide of aminopeptidase 1 protein mediates aggregation and vesicle formation in cytoplasm-to-vacuole targeting pathway. J Biol Chem. 2012 Mar 23;287(13):10121-33. doi: 10.1074/jbc.M111.311696. Epub, 2011 Nov 28. PMID:22123825 doi:http://dx.doi.org/10.1074/jbc.M111.311696
5. ↑ Frey J, Rohm KH. Subcellular localization and levels of aminopeptidases and dipeptidase in Saccharomyces cerevisiae. Biochim Biophys Acta. 1978 Nov 10;527(1):31-41. PMID:363165
6. ↑ Scott SV, Hefner-Gravink A, Morano KA, Noda T, Ohsumi Y, Klionsky DJ. Cytoplasm-to-vacuole targeting and autophagy employ the same machinery to deliver proteins to the yeast vacuole. Proc Natl Acad Sci U S A. 1996 Oct 29;93(22):12304-8. PMID:8901576
7. ↑ Scott SV, Baba M, Ohsumi Y, Klionsky DJ. Aminopeptidase I is targeted to the vacuole by a nonclassical vesicular mechanism. J Cell Biol. 1997 Jul 14;138(1):37-44. PMID:9214379
8. ↑ Baba M, Osumi M, Scott SV, Klionsky DJ, Ohsumi Y. Two distinct pathways for targeting proteins from the cytoplasm to the vacuole/lysosome. J Cell Biol. 1997 Dec 29;139(7):1687-95. PMID:9412464
9. ↑ Yamasaki A, Watanabe Y, Adachi W, Suzuki K, Matoba K, Kirisako H, Kumeta H, Nakatogawa H, Ohsumi Y, Inagaki F, Noda NN. Structural Basis for Receptor-Mediated Selective Autophagy of Aminopeptidase I Aggregates. Cell Rep. 2016 Jun 28;16(1):19-27. doi: 10.1016/j.celrep.2016.05.066. Epub 2016, Jun 16. PMID:27320913 doi:http://dx.doi.org/10.1016/j.celrep.2016.05.066