BAIT

NOS1

bNOS
nitric oxide synthase 1, neuronal
GO Process (53)
GO Function (16)
GO Component (20)

Gene Ontology Biological Process

Rattus norvegicus
PREY

HSP90AA1

EL52, HSP86, HSP89A, HSP90A, HSP90N, HSPC1, HSPCA, HSPCAL1, HSPCAL4, HSPN, Hsp89, Hsp90, LAP-2, LAP2
heat shock protein 90kDa alpha (cytosolic), class A member 1
Homo sapiens

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.

Publication

Modulation of the heme/substrate-binding cleft of neuronal nitric-oxide synthase regulates binding of Hsp90 and Hsp70 and nNOS Ubiquitination.

Peng HM, Morishima Y, Pratt WB, Osawa Y

Like other nitric-oxide synthase (NOS) enzymes, neuronal NOS (nNOS) turnover and activity are regulated by the Hsp90/Hsp70-based chaperone machinery, which regulates signaling proteins by modulating ligand binding clefts (Pratt, W.B., Morishima, Y., and Osawa, Y. (2008) J. Biol. Chem. 283, 22855-22889). We have previously shown that nNOS turnover is due to Hsp70/CHIP-dependent ubiquitination and proteasomal degradation. In this ... [more]

J. Biol. Chem. Nov. 28, 2011; 0(0); [Pubmed: 22128174]

Throughput

  • Low Throughput

Curated By

  • BioGRID