Two-hybrid

Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.

Publication

Human ASPL/TUG interacts with p97 and complements the proteasome mislocalization of a yeast ubx4 mutant, but not the ER-associated degradation defect.

Madsen L, Molbaek K, Larsen IB, Nielsen SV, Poulsen EG, Walmod PS, Hofmann K, Seeger M, Chien CY, Chen RH, Kriegenburg F, Hartmann-Petersen R

In mammalian cells, ASPL is involved in insulin-stimulated redistribution of the glucose transporter GLUT4 and assembly of the Golgi apparatus. Its putative yeast orthologue, Ubx4, is important for proteasome localization, endoplasmic reticulum-associated protein degradation (ERAD), and UV-induced degradation of RNA polymerase.Here, we show that ASPL is a cofactor of the hexameric ATPase complex, known as p97 or VCP in mammals ... [more]

BMC Cell Biol. Aug. 01, 2014; 15(0);31 [Pubmed: 25078495]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
ASPSCR1 NSF
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
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Curated By

  • BioGRID