anti-Spen Homolog, Transcriptional Regulator (Drosophila) (SPEN) Antikörper

Human Spen Homolog, Transcriptional Regulator (Drosophila) (SPEN) Interaktionspartner

1. our data demonstrate a role for SPEN in the regulation of primary cilia formation and cell migration in breast cancer cells, which may collectively explain why its expression is associated with time to metastasis in cohorts of patients with ERalpha-negative breast cancers.

2. SPEN is a novel tumor-suppressor gene that may be clinically useful as a predictive biomarker of tamoxifen response in ERalpha-positive breast cancers.

3. SPEN mutations were associated with diffuse large B-cell lymphoma with hepatitis C virus infection.

4. Phosphorylation of the CK2 site on SMRT significantly increased affinity for SHARP.

5. A structural study of the RNA binding properties of the RNA recognition motifs of SHARP.

6. These results demonstrate a role for the inactivation of SHARP transcription in DM1 biology.

7. MINT3 and MINT17 were informative for patient grouping to predict local recurrence in rectal cancer patients

8. SHARP is a novel component of the HDAC corepressor complex, recruited by RBP-Jkappa to repress transcription of target genes in the absence of activated Notch.

9. the conserved function of the SPOC domain of SHARP is to mediate interaction with SMRT/NCoR corepressors, and that Spen proteins play an essential role in the repression complex

10. both the androgen receptor interacting domains of the coactivator SRC1 and of the corepressor SMRT compete for interaction with the androgen receptor N-terminus

11. Pak1-SHARP interaction plays an essential role in enhancing the corepressor functions of SHARP, thereby modulating Notch signaling in human cancer cells.

12. Msx2-interacting protein(MINT), human interacts with the UbcH8.

13. SHARP gene and protein expression is elevated in human colon and ovarian endometrioid adenocarcinomas carrying gene defects leading to beta-catenin dysregulation.

14. In functional assays, corepressor ETO, but not AML1/ETO, augments SHARP-mediated repression in an histone deacetylase-dependent manner.

Mouse (Murine) Spen Homolog, Transcriptional Regulator (Drosophila) (SPEN) Interaktionspartner

1. Spenito, a small Spen family member, counteracted Spen function in fat regulation. Finally, mouse Spen and Spenito transcript levels scaled directly with body fat in vivo, suggesting a conserved role in fat liberation and catabolism. This study demonstrates that Spen is a key regulator of energy balance and provides a molecular context to understand the metabolic defects that arise from Spen dysfunction.

2. Spen is required for gene repression by Xist. Spen is not required for Xist RNA localization and the recruitment of chromatin modifications.

3. Spen is required for Xist-mediated silencing.

4. results suggest that Xist silences transcription by directly interacting with SHARP, recruiting SMRT, activating HDAC3, and deacetylating histones to exclude Pol II across the X chromosome

5. MINT forms a high affinity complex with CSL; the domains of MINT and CSL that are necessary and sufficient for complex formation are delineated

6. MINT plays an important role in tooth development, in particular, epithelial morphogenesis

7. Notch1 in concert with Notch2 contributes to the morphogenesis of renal vesicles into S-shaped bodies in a RBP-J-dependent manner.

8. Msx2-interacting nuclear target protein (MINT) competed with the intracellular region of Notch for binding to a DNA binding protein RBP-J and suppressed the transactivation activity of Notch signaling.

9. Stra13, Dec and Sharp (Mint) bHLH repressors are dynamically regulated during mammary gland development and may function to regulate apoptosis

10. MINT enhances Runx2 activation of multiprotein complexes assembled by the OCFRE

11. MINT is involved in CRYBP1-mediated Col2a1 gene repression and may play a role in regulation of cartilage development

12. Mint deficiency impairs differentiation of early T progenitors into double-negative cells, suggesting that Notch/RBP-J signaling negatively regulates DN1-DN2 transition