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

SEC27

L000001848, YGL137W
Essential beta'-coat protein of the COPI coatomer; involved in ER-to-Golgi and Golgi-to-ER transport; contains WD40 domains that mediate cargo selective interactions; 45% sequence identity to mammalian beta'-COP
GO Process (3)
GO Function (1)
GO Component (1)

Gene Ontology Biological Process

Gene Ontology Molecular Function

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
SEC27 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.

High4BioGRID
3611849
DSL1 SEC27
Co-localization
Co-localization

Interaction inferred from two proteins that co-localize in the cell by indirect immunofluorescence only when in addition, if one gene is deleted, the other protein becomes mis-localized. Also includes co-dependent association of proteins with promoter DNA in chromatin immunoprecipitation experiments.

Low-BioGRID
2455527
SEC27 DSL1
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
2455489

Curated By

  • BioGRID