Ligand-independent recruitment of steroid receptor coactivators to estrogen receptor by cyclin D1

Article Abstract:

Cyclin D1 has been shown to interact in a ligand-independent way with coactivators of the steroid receptor coactivator-1 (SRC-1) family in a pattern that looks like the leucine-rich coactivator binding pattern of nuclear receptors. Cyclin D1 can, through its acting as a bridging factor from SRCs and estrogen receptors (ERs), recruit SRC-family coactivators to ER where a ligand is not present. A novel route of coactivator recruitment to ER has been established as has a direct role for cyclin D1 in transcription regulation. ER is important as a regulator of both growth and differentiation for breast epithelium.

Observations, Hormone receptors, Genetic regulation, Genetic transcription, Transcription (Genetics), Estrogen, Estrogen receptors, Steroids (Drugs)

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DDB1 functions as a linker to recruit receptor WD40 proteins to CUL4-ROC1 ubiquitin ligases

Article Abstract:

A study was conducted to investigate the substrate recruiting mechanism and the architecture of DDB1-CUL4 ligases. It was seen that a protein motif, the DWD box and DDB1 act as the linker mediating DWD protein association with CUL4A and about one-third of WD40 proteins contain the DWD box suggesting a potentially large number of DWD-DDB1-CUL4-ROC1 E3 ligases.

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BRCA1 ubiquitinates its phosophorylation-dependent binding partner CtIP

Article Abstract:

Breast Cancer Susceptibility Gene 1 (BRCA1) ring domain, which catalyzes CtIP ubiquitination in a manner that depends on a phosphorylation-mediated interaction between CtIP and BRCA1 BRCT domains is demonstrated. It is proposed that BRCA1 could regulate the functions of its substrates through nonproteasomal pathways that do not involve substrate degradation.

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