Searching across hundreds of databases

Our searching services are busy right now. Your search will reload in five seconds.

Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

Selective regulation of autophagy by the Iml1-Npr2-Npr3 complex in the absence of nitrogen starvation.

Autophagy is an evolutionarily conserved pathway for the degradation of intracellular contents. How autophagy is regulated, especially upon changes in metabolic and nutritional state, remains poorly understood. By using a prototrophic strain of Saccharomyces cerevisiae, we observed that, unexpectedly, autophagy is strongly induced simply upon switch from a rich medium to a minimal medium in the complete absence of nitrogen starvation. This novel form of autophagy was termed "non-nitrogen-starvation (NNS)-induced autophagy." A visual screen uncovered three regulators of autophagy-Iml1p, Npr2p, and Npr3p-which function in the same complex and are selectively required for NNS-induced autophagy. During NNS-induced autophagy, Iml1p localized to either preautophagosomal structures (PAS) or non-PAS punctate structures. This localization suggests that Iml1p or the Iml1p-Npr2p-Npr3p complex might regulate autophagosome formation. Ultrastructural analysis confirmed that autophagosome formation was strongly impaired in Δiml1, Δnpr2, and Δnpr3 cells during NNS-induced autophagy. Moreover, Iml1p contains a conserved domain that is required for NNS-induced autophagy as well as complex formation. Collectively, our findings have revealed the existence of additional mechanisms that regulate autophagy under previously unrecognized conditions, in response to relatively more subtle changes in metabolic and nutritional state.

Pubmed ID: 21900499 RIS Download

Mesh terms: Amino Acid Sequence | Autophagy | Culture Media | Gene Knockout Techniques | Genes, Reporter | Homeostasis | Immunoprecipitation | Intracellular Signaling Peptides and Proteins | Microscopy, Fluorescence | Molecular Sequence Data | Multiprotein Complexes | Nitrogen | Phenotype | Phosphorylation | Protein Binding | Protein Structure, Tertiary | Saccharomyces cerevisiae | Saccharomyces cerevisiae Proteins

Research resources used in this publication

None found

Research tools detected in this publication

None found

Data used in this publication

None found

Associated grants

  • Agency: NIGMS NIH HHS, Id: R01 GM094314
  • Agency: NIGMS NIH HHS, Id: R01GM094314
  • Agency: Howard Hughes Medical Institute, Id:

Publication data is provided by the National Library of Medicine ® and PubMed ®. Data is retrieved from PubMed ® on a weekly schedule. For terms and conditions see the National Library of Medicine Terms and Conditions.

We have not found any resources mentioned in this publication.