BAIT

SMY2

L000001941, YBR172C
GYF domain protein; involved in COPII vesicle formation; interacts with the Sec23p/Sec24p subcomplex; overexpression suppresses the temperature sensitivity of a myo2 mutant; similar to S. pombe Mpd2; SMY2 has a paralog, SYH1, that arose from the whole genome duplication
GO Process (1)
GO Function (0)
GO Component (4)
Saccharomyces cerevisiae (S288c)
PREY

EAP1

YKL204W
eIF4E-associated protein, competes with eIF4G for binding to eIF4E; accelerates mRNA degradation by promoting decapping, facilitated by interaction with eIF4E; essential for Puf5p mediated repression; associates with Puf5p and Dhh1p; inhibits cap-dependent translation; functions independently of eIF4E to maintain genetic stability; plays a role in cell growth, implicated in the TOR signaling cascade
Saccharomyces cerevisiae (S288c)

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.

Publication

Conserved beta-hairpin recognition by the GYF domains of Smy2 and GIGYF2 in mRNA surveillance and vesicular transport complexes.

Ash MR, Faelber K, Kosslick D, Albert GI, Roske Y, Kofler M, Schuemann M, Krause E, Freund C

The yeast suppressor of myosin 2 protein (Smy2) interacts with mRNA-processing proteins through recognition of proline-rich sequences (PRS). Here, we describe the crystal structure of the GYF domain of Smy2 in association with a PRS from the yeast branch point binding protein (BBP/ScSF1). Complex formation requires that the beta-hairpin of the central PPGL motif of the ligand is accommodated by ... [more]

Structure Aug. 11, 2010; 18(8);944-54 [Pubmed: 20696395]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
SMY2 EAP1
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.

High-BioGRID
-
SMY2 EAP1
Affinity Capture-Western
Affinity Capture-Western

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 identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.

Low-BioGRID
-
EAP1 SMY2
Affinity Capture-Western
Affinity Capture-Western

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 identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.

Low-BioGRID
-
SMY2 EAP1
Synthetic Lethality
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.

Low-BioGRID
349830

Curated By

  • BioGRID