BAIT

DSL1

RNS1, L000004950, YNL258C
Peripheral membrane protein needed for Golgi-to-ER retrograde traffic; mediates Sey1p-independent homotypic ER fusion; forms a complex with Sec39p and Tip20p that interacts with ER SNAREs Sec20p and Use1p; component of the ER target site that interacts with coatomer; interacts with Cin5p; similar to the fly and human ZW10 gene
GO Process (2)
GO Function (0)
GO Component (4)

Gene Ontology Biological Process

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)
PREY

SEC28

ANU2, L000004402, YIL076W
Epsilon-COP subunit of the coatomer; regulates retrograde Golgi-to-ER protein traffic; stabilizes Cop1p, the alpha-COP and the coatomer complex; non-essential for cell growth; protein abundance increases in response to DNA replication stress
GO Process (3)
GO Function (0)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)

Synthetic Lethality

A genetic interaction is inferred when mutations or deletions in separate genes, each of which alone causes a minimal phenotype, result in lethality when combined in the same cell under a given condition.

Publication

ER arrival sites for COPI vesicles localize to hotspots of membrane trafficking.

Schroeter S, Beckmann S, Schmitt HD

COPI-coated vesicles mediate retrograde membrane traffic from the cis-Golgi to the endoplasmic reticulum (ER) in all eukaryotic cells. However, it is still unknown whether COPI vesicles fuse everywhere or at specific sites with the ER membrane. Taking advantage of the circumstance that the vesicles still carry their coat when they arrive at the ER, we have visualized active ER arrival ... [more]

EMBO J. Sep. 01, 2016; 35(17);1935-55 [Pubmed: 27440402]

Throughput

  • Low Throughput

Ontology Terms

  • phenotype: inviable (APO:0000112)

Additional Notes

  • the dsl1 mutations are lethal in the presence of the VN tag fused to the C-terminus of COPI subunits, alpha-, beta prime-, epsilon-, or delta-COP

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
SEC28 DSL1
Affinity Capture-MS
Affinity Capture-MS

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.

High2BioGRID
3611866
DSL1 SEC28
PCA
PCA

A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay.

Low-BioGRID
2455487
SEC28 DSL1
Protein-peptide
Protein-peptide

An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments.

Low-BioGRID
-

Curated By

  • BioGRID