Reconstitution of the KRAB-KAP-1 repressor complex: a model system for defining the molecular anatomy of RING-B box-coiled-coil domain-mediated protein-protein interactions

Peng, Hongzhuang; Begg, Gillian E.; Schultz, D.; Friedman, Josh R.; Jensen, David E.; Speicher, David W.; Rauscher, Frank J.

doi:10.1006/jmbi.1999.3402

Cited by 180 publications

(165 citation statements)

References 58 publications

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“…The bases for this difference are unknown. KRABZFPs recruit KAP1 as a trimer (Peng et al 2000). Whether similar high-order KAP1 complexes are formed at MyoD/ Mef2D-bearing loci remains to be determined, but it would certainly allow for the assembly of a large platform spanning multiple transcription modulators at CRMs, consistent with our observations that an extensive group Figure 6.…”

Section: Discussionsupporting

confidence: 80%

A KAP1 phosphorylation switch controls MyoD function during skeletal muscle differentiation

et al. 2015

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The transcriptional activator MyoD serves as a master controller of myogenesis. Often in partnership with Mef2 (myocyte enhancer factor 2), MyoD binds to the promoters of hundreds of muscle genes in proliferating myoblasts yet activates these targets only upon receiving cues that launch differentiation. What regulates this off/on switch of MyoD function has been incompletely understood, although it is known to reflect the action of chromatin modifiers. Here, we identify KAP1 (KRAB [Kr€ uppel-like associated box]-associated protein 1)/TRIM28 (tripartite motif protein 28) as a key regulator of MyoD function. In myoblasts, KAP1 is present with MyoD and Mef2 at many muscle genes, where it acts as a scaffold to recruit not only coactivators such as p300 and LSD1 but also corepressors such as G9a and HDAC1 (histone deacetylase 1), with promoter silencing as the net outcome. Upon differentiation, MSK1-mediated phosphorylation of KAP1 releases the corepressors from the scaffold, unleashing transcriptional activation by MyoD/Mef2 and their positive cofactors. Thus, our results reveal KAP1 as a previously unappreciated interpreter of cell signaling, which modulates the ability of MyoD to drive myogenesis.

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Section: Discussionsupporting

confidence: 80%

A KAP1 phosphorylation switch controls MyoD function during skeletal muscle differentiation

et al. 2015

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“…Both silver nitrate staining and sequential immunoprecipitations are consistent with the existence of two related complexes, a major TRIM33 and TRIM24 complex and a second less abundant complex additionally containing TRIM28. It has previously been shown that TRIM24 and TRIM33 can interact via their RBCC domain (42,43), however it remains to be determined whether TRIM28 interacts directly with TRIM24 and/or TRIM33 or whether it associates with the complex via interactions with other subunits. Similarly, it is possible that the core histones, HP1 proteins and HDACs associate with the complex via interactions with TRIM24 or via a combination of all three TRIM subunits.…”

Section: Hepatocyte-specific Trim24 Inactivation Increases Proliferatmentioning

confidence: 99%

Transcription cofactors TRIM24, TRIM28, and TRIM33 associate to form regulatory complexes that suppress murine hepatocellular carcinoma

Herquel

Ouararhni

Khetchoumian

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

179

160

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TRIM24 (TIF1α), TRIM28 (TIF1β), and TRIM33 (TIF1γ) are three related cofactors belonging to the tripartite motif superfamily that interact with distinct transcription factors. TRIM24 interacts with the liganded retinoic acid (RA) receptor to repress its transcriptional activity. Germ line inactivation of TRIM24 in mice deregulates RA-signaling in hepatocytes leading to the development of hepatocellular carcinoma (HCC). Here we show that TRIM24 can be purified as at least two macromolecular complexes comprising either TRIM33 or TRIM33 and TRIM28. Somatic hepatocyte-specific inactivation of TRIM24, TRIM28, or TRIM33 all promote HCC in a cell-autonomous manner in mice. Moreover, HCC formation upon TRIM24 inactivation is strongly potentiated by further loss of TRIM33. These results demonstrate that the TIF1-related subfamily of TRIM proteins interact both physically and functionally to modulate HCC formation in mice.

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“…KAP1/TRIM28/TIF1␤ contains multiple functional domains. It has a RING finger at the N terminus followed by B-Boxes and coiled coil domains (34,35). It also has an HP1-binding motif in the middle (36 -38).…”

mentioning

confidence: 99%

Zinc Finger Protein ZFP57 Requires Its Co-factor to Recruit DNA Methyltransferases and Maintains DNA Methylation Imprint in Embryonic Stem Cells via Its Transcriptional Repression Domain

Zuo

Sheng

Lau

et al. 2012

Journal of Biological Chemistry

155

171

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Background: ZFP57 is a maternal-zygotic effect gene that maintains genomic imprinting in mouse embryos. Results: KAP1 facilitates the interaction between ZFP57 and DNA methyltransferases. The KRAB box of ZFP57 is required for maintaining DNA methylation imprint in ES cells. Conclusion: ZFP57 recruits DNA methyltransferases and maintains DNA methylation imprint through KRAB box-mediated interaction.Significance: This work implies that ZFP57 recruits DNA methyltransferases via KAP1 to maintain DNA methylation imprint.

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Reconstitution of the KRAB-KAP-1 repressor complex: a model system for defining the molecular anatomy of RING-B box-coiled-coil domain-mediated protein-protein interactions

Cited by 180 publications

References 58 publications

A KAP1 phosphorylation switch controls MyoD function during skeletal muscle differentiation

A KAP1 phosphorylation switch controls MyoD function during skeletal muscle differentiation

Transcription cofactors TRIM24, TRIM28, and TRIM33 associate to form regulatory complexes that suppress murine hepatocellular carcinoma

Zinc Finger Protein ZFP57 Requires Its Co-factor to Recruit DNA Methyltransferases and Maintains DNA Methylation Imprint in Embryonic Stem Cells via Its Transcriptional Repression Domain

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