Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10801938 | Biochimica et Biophysica Acta (BBA) - Molecular Cell Research | 2015 | 9 Pages |
Abstract
Steroid receptor coactivator 2 (SRC-2) is a coactivator that regulates nuclear receptor activity. We previously reported that SRC-2 protein is degraded through the action of cAMP-dependent protein kinase A (PKA) and cAMP response element binding protein (CREB). In the study presented here, we aimed to identify proteins that interact with and thereby regulate SRC-2. We isolated cyclin C (CCNC) as an interacting partner with the SRC-2 degradation domain aa 347-758 in a yeast two-hybrid assay and confirmed direct interaction in an in vitro assay. The protein level of SRC-2 was increased with CCNC overexpression in COS-1 cells and decreased with CCNC silencing in COS-1 and MCF-7 cells. In a pulse-chase assay, we further show that silencing of CCNC resulted in a different SRC-2 degradation pattern during the first 6Â h after the pulse. Finally, we provide evidence that CCNC regulates expression of cell cycle genes upregulated by SRC-2. In conclusion, our results suggest that CCNC temporarily protects SRC-2 against degradation and this event is involved in the transcriptional regulation of SRC-2 cell cycle target genes.
Keywords
ERαTIF2chemokine (C-X-C motif) receptor 4Coding DNAGRIP1Cyclin CCCNCNR2F2MCM7EGR1CHXCXCR4pKaSRCY2HBcl-2SDSFBSGAPDHTBPNSC17β-estradiolcAMPCdk6cDNASmall interfering RNAsiRNACyclic adenosine monophosphateAmino acidshexahistidine tagEMTsodium dodecyl sulfatefetal bovine serumcycloheximidecyclin-dependent kinase 6LynMybYeast two hybridhemagglutininMediatorquantitative real-time PCRearly growth response 1TATA box binding proteinprotein kinase AEpithelial–mesenchymal transitionglyceraldehyde-3-phosphate dehydrogenaseEstrogen receptor alpha
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Authors
Olivera Bozickovic, Tuyen Hoang, Ingvild S. Fenne, Thomas Helland, Linn Skartveit, Mamoru Ouchida, Gunnar Mellgren, Jørn V. Sagen,