Abstract：
:Tribbles 3 homolog (TRB3) is recently identified as a scaffold-like regulator of various signal transducers and has been implicated in several processes including insulin signaling, NF-kappaB signaling, lipid metabolism and BMP signaling. To further understand cellular mechanisms of TRB3 regulation, we performed a yeast two-hybrid screen to identify novel TRB3 interacting proteins and totally obtained ten in-frame fused preys. Candidate interactions were validated by co-immunoprecipitation assays in mammalian cells. We further characterized the identified proteins sorted by Gene Ontology Annotation. Its interaction with the E3 ubiquitin ligase SIAH1 was further investigated. SIAH1 could interact with TRB3 both in vitro and in vivo. Importantly, SIAH1 targeted TRB3 for proteasome-dependent degradation. Cotransfection of SIAH1 could withdraw up-regulation of TGF-beta signaling by TRB3, suggesting SIAH1-induced degradation of TRB3 represents a potential regulatory mechanism for TGF-beta signaling.
journal_name
Cell Signaljournal_title
Cellular signallingauthors
Zhou Y,Li L,Liu Q,Xing G,Kuai X,Sun J,Yin X,Wang J,Zhang L,He Fdoi
10.1016/j.cellsig.2008.01.010subject
Has Abstractpub_date
2008-05-01 00:00:00pages
942-8issue
5eissn
0898-6568issn
1873-3913pii
S0898-6568(08)00027-2journal_volume
20pub_type
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