ArticleThe Journal of cell biology1996
Identification of a cytoplasm to vacuole targeting determinant in aminopeptidase I.
Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 103 citations in OpenAlex.
- The autophagy-specific exocyst subcomplex contributes to phagophore assembly site integrity by promoting phagophore expansion.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Two aminopeptidase I homologs convergently contribute to pathobiology of fungal entomopathogen Beauveria bassiana via divergent physiology-dependent autophagy pathways for vacuolar targeting.Journal of advanced research · 2024Article
- Gene Organization, Expression, and Localization of Ribotoxin-Like Protein Ageritin in Fruiting Body and Mycelium ofInternational journal of molecular sciences · 2020Article
- Liquid-liquid phase separation in autophagy.The Journal of cell biology · 2020Review
- Higher-order assemblies of oligomeric cargo receptor complexes form the membrane scaffold of the Cvt vesicle.EMBO reports · 2016Article
- Vacuolar targeting of r-proteins in sugarcane leads to higher levels of purifiable commercially equivalent recombinant proteins in cane juice.Plant biotechnology journal · 2016Article
- Article
- The machinery of macroautophagy.Cell research · 2014Review
- Review
- Selective autophagy in budding yeast.Cell death and differentiation · 2013Review
- Propeptide of aminopeptidase 1 protein mediates aggregation and vesicle formation in cytoplasm-to-vacuole targeting pathway.The Journal of biological chemistry · 2012Article
- Proteomic and biochemical evidence support a role for transport vesicles and endosomes in stress response and secondary metabolism in Aspergillus parasiticus.Journal of proteome research · 2012Article
- The Cytoplasm-to-Vacuole Targeting Pathway: A Historical Perspective.International journal of cell biology · 2012Article
- Compartmentalization and molecular traffic in secondary metabolism: a new understanding of established cellular processes.Fungal genetics and biology : FG & B · 2011Review
- The Cvt pathway as a model for selective autophagy.FEBS letters · 2010Review
- An overview of the molecular mechanism of autophagy.Current topics in microbiology and immunology · 2009Review
- Leishmania lysosomal targeting signal is recognized by yeast and not by mammalian cells.Parasitology research · 2008Article
- Crystallization of Saccharomyces cerevisiae aminopeptidase 1, the major cargo protein of the Cvt pathway.Acta crystallographica. Section F, Structural biology and crystallization communications · 2007Article
- Recruitment of Atg9 to the preautophagosomal structure by Atg11 is essential for selective autophagy in budding yeast.The Journal of cell biology · 2006Article
- The actin cytoskeleton is required for selective types of autophagy, but not nonspecific autophagy, in the yeast Saccharomyces cerevisiae.Molecular biology of the cell · 2005Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Aminopeptidase I (API) is a soluble leucine aminopeptidase resident in the yeast vacuole (Frey, J., and K.H. Rohm. 1978. Biochim. Biophys. Acta. 527:31-41). The precursor form of API contains an amino-terminal 45-amino acid propeptide, which is removed by proteinase B (PrB) upon entry into the vacuole. The propeptide of API lacks a consensus signal sequence and it has been demonstrated that vacuolar localization of API is independent of the secretory pathway (Klionsky, D.J., R. Cueva, and D.S. Yaver. 1992. J. Cell Biol. 119:287-299). The predicted secondary structure for the API propeptide is composed of an amphipathic alpha-helix followed by a beta-turn and another alpha-helix, forming a helix-turn-helix structure. With the use of mutational analysis, we determined that the API propeptide is essential for proper transport into the vacuole. Deletion of the entire propeptide from the API molecule resulted in accumulation of a mature-sized protein in the cytosol. A more detailed examination using random mutagenesis and a series of smaller deletions throughout the propeptide revealed that API localization is severely affected by alterations within the predicted first alpha-helix. In vitro studies indicate that mutations in this predicted helix prevent productive binding interactions from taking place. In contrast, vacuolar import is relatively insensitive to alterations in the second predicted helix of the propeptide. Examination of API folding revealed that mutations that affect entry into the vacuole did not affect the structure of API. These data indicate that the API propeptide serves as a vacuolar targeting determinant at a critical step along the cytoplasm to vacuole targeting pathway.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.