BAIT

CCT3

BIN2, TCP3, L000002270, YJL014W
Subunit of the cytosolic chaperonin Cct ring complex; related to Tcp1p, required for the assembly of actin and tubulins in vivo; capable of binding Q/N rich proteins and mediating their folding
GO Process (1)
GO Function (1)
GO Component (1)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

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

The interaction network of the chaperonin CCT.

Dekker C, Stirling PC, McCormack EA, Filmore H, Paul A, Brost RL, Costanzo M, Boone C, Leroux MR, Willison KR

The eukaryotic cytosolic chaperonin containing TCP-1 (CCT) has an important function in maintaining cellular homoeostasis by assisting the folding of many proteins, including the cytoskeletal components actin and tubulin. Yet the nature of the proteins and cellular pathways dependent on CCT function has not been established globally. Here, we use proteomic and genomic approaches to define CCT interaction networks involving ... [more]

EMBO J. Jul. 09, 2008; 27(13);1827-39 [Pubmed: 18511909]

Throughput

  • High Throughput

Curated By

  • BioGRID