Academic Journal
Yeast Npi3/Bro1 is involved in ubiquitin-dependent control of permease trafficking.
| العنوان: | Yeast Npi3/Bro1 is involved in ubiquitin-dependent control of permease trafficking. |
|---|---|
| المؤلفون: | Springael, Jean-Yves, Nikko, Elina, André, Bruno, Marini, Anna Maria |
| المصدر: | FEBS letters, 517 (1-3 |
| سنة النشر: | 2002 |
| المجموعة: | DI-fusion : dépôt institutionnel de l'Université libre de Bruxelles (ULB) |
| مصطلحات موضوعية: | Sciences bio-médicales et agricoles, Animals, Biological Transport, Cloning, Molecular, Conserved Sequence -- genetics, Down-Regulation, Endosomes -- metabolism, Eukaryotic Cells -- metabolism, Fungal Proteins -- chemistry, Fungal Proteins -- genetics, Fungal Proteins -- metabolism, Humans, Membrane Transport Proteins -- metabolism, Monosaccharide Transport Proteins -- metabolism, Nucleotide Transport Proteins, Protein Structure, Tertiary, Protein Transport -- physiology, Saccharomyces cerevisiae Proteins -- metabolism, Ubiquitin -- metabolism, Vacuoles -- metabolism, Yeasts -- metabolism, alpha Karyopherins -- chemistry, alpha Karyopherins -- genetics, alpha Karyopherins -- metabolism, Npi3/Bro1, Permease, Traffic, Ubiquitin |
| الوصف: | The membrane traffic and stability of the general amino acid permease Gap1 of Saccharomyces cerevisiae are under nitrogen control. Addition of a preferential nitrogen source such as ammonium to cells growing on a poor nitrogen source induces internalization of the permease and its subsequent degradation in the vacuole. This down-regulation requires ubiquitination of Gap1 through a process involving ubiquitin ligase Npi1/Rsp5, ubiquitin hydrolase Npi2/Doa4, and Bul1/2, two Npi1/Rsp5 interacting proteins. Here we report that yet another protein, Npi3, is involved in the regulation of Gap1 trafficking. We show that Npi3 is required for NH4+-induced down-regulation of Gap1, and particularly for efficient ubiquitination of the permease. Npi3 plays a pleiotropic role in permease down-regulation, since it is also involved in ubiquitination and stress-induced down-regulation of the uracil permease Fur4 and in glucose-induced degradation of hexose transporters Hxt6/7. We further provide evidence that Npi3 is required for direct vacuolar sorting of neosynthesized Gap1 permease as it occurs in npr1 mutant cells. NPI3 is identical to BRO1, a gene encoding a protein of unknown biochemical function and recently proposed to be involved in protein turnover. Npi3/Bro1 homologues include fungal proteins required for proteolytic cleavage of zinc finger proteins and the mouse Aip1 protein involved in apoptosis. We propose that proteins of the Npi3/Bro1 family, including homologues from higher species, may play a conserved role in ubiquitin-dependent control of membrane protein trafficking. ; Journal Article ; Research Support, Non-U.S. Gov't ; info:eu-repo/semantics/published |
| نوع الوثيقة: | article in journal/newspaper |
| وصف الملف: | 1 full-text file(s): application/pdf |
| اللغة: | English |
| Relation: | uri/info:doi/10.1016/S0014-5793(02)02586-3; uri/info:pii/S0014579302025863; uri/info:pmid/12062418; uri/info:scp/0037165612; https://dipot.ulb.ac.be/dspace/bitstream/2013/51711/1/Elsevier_26831.pdf; http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/51711 |
| الاتاحة: | http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/51711 https://dipot.ulb.ac.be/dspace/bitstream/2013/51711/1/Elsevier_26831.pdf |
| رقم الانضمام: | edsbas.D9AD0591 |
| قاعدة البيانات: | BASE |
| الوصف غير متاح. |