BAIT

MIC60

AIM28, FCJ1, FMP13, YKR016W
Component of the MICOS complex; MICOS (formerly MINOS or MitOS) is a mitochondrial inner membrane complex that extends into the intermembrane space and has a role in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane; Mic60p is also involved in import of intermembrane space (IMS) proteins, probably by positioning Mia40p relative to the TOM complex to receive incoming proteins; ortholog of mammalian mitofilin
GO Process (2)
GO Function (0)
GO Component (5)
Saccharomyces cerevisiae (S288c)
PREY

SCO1

PET161, L000001815, YBR037C
Copper-binding protein of mitochondrial inner membrane; required for cytochrome c oxidase activity and respiration; may function to deliver copper to cytochrome c oxidase; similar to thioredoxins; SCO1 has a paralog, SCO2, that arose from the whole genome duplication
GO Process (3)
GO Function (2)
GO Component (2)
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

Coordination of cytochrome bc1 complex assembly at MICOS.

Zerbes RM, Colina-Tenorio L, Bohnert M, von der Malsburg K, Peikert CD, Mehnert CS, Perschil I, Klar RFU, de Boer R, Kram A, van der Klei I, Oeljeklaus S, Warscheid B, Rampelt H, van der Laan M

The boundary and cristae domains of the mitochondrial inner membrane are connected by crista junctions. Most cristae membrane proteins are nuclear-encoded and inserted by the mitochondrial protein import machinery into the inner boundary membrane. Thus, they must overcome the diffusion barrier imposed by crista junctions to reach their final location. Here, we show that respiratory chain complexes and assembly intermediates ... [more]

EMBO Rep Jan. 01, 2025; 26(2);353-384 [Pubmed: 39623166]

Throughput

  • High Throughput

Curated By

  • BioGRID