BAIT

HSP104

chaperone ATPase HSP104, L000000823, YLL026W
Disaggregase; heat shock protein that cooperates with Ydj1p (Hsp40) and Ssa1p (Hsp70) to refold and reactivate previously denatured, aggregated proteins; responsive to stresses including: heat, ethanol, and sodium arsenite; involved in [PSI+] propagation; protein becomes more abundant and forms cytoplasmic foci in response to DNA replication stress; potentiated Hsp104p variants decrease TDP-43 proteotoxicity by eliminating its cytoplasmic aggregation
Saccharomyces cerevisiae (S288c)
PREY

CKA1

casein kinase 2 catalytic subunit CKA1, L000000343, YIL035C
Alpha catalytic subunit of casein kinase 2 (CK2); a Ser/Thr protein kinase with roles in cell growth and proliferation; CK2, comprised of CKA1, CKA2, CKB1 and CKB2, has many substrates including transcription factors and all RNA polymerases; regulates Fkh1p-mediated donor preference during mating-type switching
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

Nuclear Hsp104 safeguards the dormant translation machinery during quiescence.

Kohler V, Kohler A, Berglund LL, Hao X, Gersing S, Imhof A, Nystroem T, Hoeoeg JL, Ott M, Andreasson C, Buettner S

The resilience of cellular proteostasis declines with age, which drives protein aggregation and compromises viability. The nucleus has emerged as a key quality control compartment that handles misfolded proteins produced by the cytosolic protein biosynthesis system. Here, we find that age-associated metabolic cues target the yeast protein disaggregase Hsp104 to the nucleus to maintain a functional nuclear proteome during quiescence. ... [more]

Nat Commun Jan. 05, 2024; 15(1);315 [Pubmed: 38182580]

Throughput

  • Low Throughput

Curated By

  • BioGRID