The presence of multiple membrane-bound intracellular compartments is a major feature of eukaryotic cells. Many of the proteins required for formation and maintenance of these compartments share an evolutionary history. Here, we identify the SEA (Seh1-associated) protein complex in yeast that contains the nucleoporin Seh1 and Sec13, the latter subunit of both the nuclear pore complex and the COPII coating complex. The SEA complex also contains Npr2 and Npr3 proteins (upstream regulators of TORC1 kinase) and four previously uncharacterized proteins (Sea1-Sea4). Combined computational and biochemical approaches indicate that the SEA complex proteins possess structural characteristics similar to the membrane coating complexes COPI, COPII, the nuclear pore complex, and, in particular, the related Vps class C vesicle tethering complexes HOPS and CORVET. The SEA complex dynamically associates with the vacuole in vivo. Genetic assays indicate a role for the SEA complex in intracellular trafficking, amino acid biogenesis, and response to nitrogen starvation. These data demonstrate that the SEA complex is an additional member of a family of membrane coating and vesicle tethering assemblies, extending the repertoire of protocoatomer-related complexes.
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| Gene/Complex | Qualifier | Gene Ontology Term | Annotation Extension | Evidence | Source | Assigned On |
|---|---|---|---|---|---|---|
| SEA4 | part of | Seh1-associated complex | IDA | SGD | 2013-08-07 | |
| MTC5 | part of | Seh1-associated complex | IDA | SGD | 2013-08-07 | |
| NPR2 | part of | Seh1-associated complex | IDA | SGD | 2013-08-07 | |
| SEH1 | part of | Seh1-associated complex | IDA | SGD | 2013-08-07 | |
| NPR3 | part of | Seh1-associated complex | IDA | SGD | 2013-08-07 | |
| IML1 | part of | Seh1-associated complex | IDA | SGD | 2013-08-07 | |
| SEC13 | part of | Seh1-associated complex | IDA | SGD | 2013-08-07 | |
| RTC1 | part of | Seh1-associated complex | IDA | SGD | 2013-08-07 |
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| Gene | Phenotype | Experiment Type | Mutant Information | Strain Background | Chemical | Details |
|---|---|---|---|---|---|---|
| NPR2 | autophagy: decreased Reporter: GFP-Atg8p | classical genetics | null Allele: npr2-Δ | S288C | Media: nitrogen starvation Details: Atg8p is blocked in the cytoplasm, rather than being localized to the vacuole after nitrogen starvation | |
| NPR3 | autophagy: decreased Reporter: GFP-Atg8p | classical genetics | null Allele: npr3-Δ | S288C | Media: nitrogen starvation Details: Atg8p is equally distributed between the vacuole and cytoplasm, rather than being exclusively localized to the vacuole after nitrogen starvation |
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| Evidence ID | Analyze ID | Interactor | Interactor Systematic Name | Interactor | Interactor Systematic Name | Allele | Assay | Annotation | Action | Phenotype | SGA score | P-value | Source | Reference | Note |
|---|
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| Interactor | Interactor | Assay | Annotation | Action | Modification | |
|---|---|---|---|---|---|---|
| IML1 | RTC1 | Affinity Capture-MS | manually curated | Bait-Hit | No Modification | |
| IML1 | SEC13 | Affinity Capture-MS | manually curated | Bait-Hit | No Modification | |
| IML1 | RTC1 | Affinity Capture-MS | manually curated | Hit-Bait | No Modification | |
| MTC5 | SEH1 | Affinity Capture-MS | manually curated | Hit-Bait | No Modification | |
| MTC5 | IML1 | Affinity Capture-MS | manually curated | Hit-Bait | No Modification | |
| MTC5 | RTC1 | Affinity Capture-MS | manually curated | Hit-Bait | No Modification | |
| MTC5 | IML1 | Affinity Capture-MS | manually curated | Bait-Hit | No Modification | |
| MTC5 | RTC1 | Affinity Capture-MS | manually curated | Bait-Hit | No Modification | |
| MTC5 | SEH1 | Affinity Capture-MS | manually curated | Bait-Hit | No Modification | |
| MTC5 | SEC13 | Affinity Capture-MS | manually curated | Bait-Hit | No Modification |