IndraLab

Statements


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"2A-DUB interacts with p/CAF in a coregulatory protein complex, with its deubiquitinase activity modulated by the status of acetylation of nucleosomal histones."

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"Interestingly, 2A-DUB associates with PCAF, a histone acetyltransferase subunit of the hSAGA complex."

No evidence text available

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"Correlating with the recruitment of 2A-DUB and p/CAF, a clear decrease of uH2A levels and a coincidently increased level of acetylated H3 (Ac-H3) were observed upon DHT treatment in LNCaP cells, sugge[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

No evidence text available

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"2A-DUB interacts with PCAF and is required for full activation of androgen receptor-dependent genes (Zhu et al., xref )."

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"Displacement of linker histones, which is facilitated by their phosphorylation, is generally linked to gene activation but has also been linked to repression in a few instances, coincident with the co[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"2A-DUB interacts with PCAF and is required for full activation of androgen receptor dependent genes."

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"Unexpectedly, specific interactions between p/CAF and 2A-DUB, as components of a protein complex, seem to coordinate histone ubiquitination and acetylation."

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"Coimmunoprecipitation assays further confirmed a specific interaction of 2A-DUB with p/CAF, as well as interactions with R NA- b inding m otif protein 10 (RBM10) and t hyroid hormone r eceptor ([MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"The HAT P/CAF physically interacts with the DUB Mysm1 ( xref ); however, whether DUBs play a role in the regulation of HAT stability is unclear."

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"2A-DUB interacts with p/CAF in a coregulatory protein complex, with its deubiquitinase activity modulated by the status of acetylation of nucleosomal histones."

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"The interacting partners 2A-DUB and PCAF, are recruited to the promoter region, remove the uH2A repressive mark and facilitate the dissociation of linker proteins, creating an open chromatin environment."