PBAF lacking PHD domains maintains transcription in human neutrophils

Viryasova, Galina M.; Tatarskiy, Victor V.; Sheynov, A A; Tatarskiy, E V; Sud’ina, Galina F.; Георгиева, С. Г.; Сошникова, Н. В.

doi:10.1016/j.bbamcr.2019.118525

Cited by 9 publications

(14 citation statements)

References 37 publications

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“…PHF10 is required for the maintenance of long-term repopulating hematopoietic stem cells [ 21 ]. PHF10-P isoforms are highly expressed in actively proliferating myelocytes [ 19 ]. Induced knockout of PHF10 in transgenic mice leads to a decrease of the myeloid progenitor pool in the bone marrow.…”

Section: The Role Of Phf10 Isoforms In Gene Transcriptionmentioning

confidence: 99%

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Conserved Structure and Evolution of DPF Domain of PHF10—The Specific Subunit of PBAF Chromatin Remodeling Complex

Chugunov

Potapova

Klimenko

et al. 2021

IJMS

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Transcription activation factors and multisubunit coactivator complexes get recruited at specific chromatin sites via protein domains that recognize histone modifications. Single PHDs (plant homeodomains) interact with differentially modified H3 histone tails. Double PHD finger (DPF) domains possess a unique structure different from PHD and are found in six proteins: histone acetyltransferases MOZ and MORF; chromatin remodeling complex BAF (DPF1–3); and chromatin remodeling complex PBAF (PHF10). Among them, PHF10 stands out due to the DPF sequence, structure, and functions. PHF10 is ubiquitously expressed in developing and adult organisms as four isoforms differing in structure (the presence or absence of DPF) and transcription regulation functions. Despite the importance of the DPF domain of PHF10 for transcription activation, its structure remains undetermined. We performed homology modeling of the human PHF10 DPF domain and determined common and distinct features in structure and histone modifications recognition capabilities, which can affect PBAF complex chromatin recruitment. We also traced the evolution of DPF1–3 and PHF10 genes from unicellular to vertebrate organisms. The data reviewed suggest that the DPF domain of PHF10 plays an important role in SWI/SNF-dependent chromatin remodeling during transcription activation.

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Section: The Role Of Phf10 Isoforms In Gene Transcriptionmentioning

confidence: 99%

“…Furthermore, PHF10 functions and its role in transcriptional regulation are also unique. Mammalians have four PHF10 alternative splicing isoforms, which possess distinct domain structures and play different roles in gene transcription [ 17 , 18 , 19 ].…”

Section: Introductionmentioning

confidence: 99%

Conserved Structure and Evolution of DPF Domain of PHF10—The Specific Subunit of PBAF Chromatin Remodeling Complex

Chugunov

Potapova

Klimenko

et al. 2021

IJMS

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“…Показано, что белок PHF10 в составе комплекса PBAF коактивирует транскрипцию различных генов [38,39]. Получены прямые доказательства необходимости DPF-домена белка PHF10 для активации транскрипции, так как без DPF белок не способен активировать транскрипцию [38,40]. Интересно, что в клетке также существует изоформа PHF10, не имеющая DPFдомена [39].…”

Section: Dpf взаимодействуют с ацилированными H3k14 и H3k9unclassified

“…Интересно, что в клетке также существует изоформа PHF10, не имеющая DPFдомена [39]. Показано, что изоформа с DPF-доменом участвует в активации транскрипции, тогда как изоформа без DPF необходима для поддержания стабильного уровня транскрипции после активации [40]. Таким образом, DPF-домен белка PHF10 является сильным коактиватором транскрипции.…”

Section: Dpf взаимодействуют с ацилированными H3k14 и H3k9unclassified

“…В исследовании, выполненном на модельной линии HL-60, способной дифференцироваться по миелоидному ряду, и на терминально дифференцированных нейтрофилах человека, установлено, что важную роль в поддержании пролиферирующих миелоидных предшественников играют изоформы PHF10 с доменом DPF, также необходимые для активации специфических миелоидных генов, экспрессия которых активируется при дифференцировке. В зрелых нейтрофилах транскрипцию специфических генов поддерживают изоформы PHF10, не имеющие DPF [40]. [60], а недостаток этого белка ведет к развитию сценария старения нейрональных стволовых клеток [43].…”

Section: Dpf взаимодействуют с ацилированными H3k14 и H3k9unclassified

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The DPF Domain As a Unique Structural Unit Participating in Transcriptional Activation, Cell Differentiation, and Malignant Transformation

et al. 2020

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The DPF (double PHD finger) domain consists of two PHD fingers organized in tandem. The two PHD-finger domains within a DPF form a single structure that interacts with the modification of the N-terminal histone fragment in a way different from that for single PHD fingers. Several histone modifications interacting with the DPF domain have already been identified. They include acetylation of H3K14 and H3K9, as well as crotonylation of H3K14. These modifications are found predominantly in transcriptionally active chromatin. Proteins containing DPF belong to two classes of protein complexes, which are the transcriptional coactivators involved in the regulation of the chromatin structure. These are the histone acetyltransferase complex belonging to the MYST family and the SWI/SNF chromatin-remodeling complex. The DPF domain is responsible for the specificity of the interactions between these complexes and chromatin. Proteins containing DPF play a crucial role in the activation of the transcription of a number of genes expressed during the development of an organism. These genes are important in the differentiation and malignant transformation of mammalian cells.

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ZC3H13-mediated N6-methyladenosine modification of PHF10 is impaired by fisetin which inhibits the DNA damage response in pancreatic cancer

et al. 2022

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PBAF lacking PHD domains maintains transcription in human neutrophils

Cited by 9 publications

References 37 publications

Conserved Structure and Evolution of DPF Domain of PHF10—The Specific Subunit of PBAF Chromatin Remodeling Complex

Conserved Structure and Evolution of DPF Domain of PHF10—The Specific Subunit of PBAF Chromatin Remodeling Complex

The DPF Domain As a Unique Structural Unit Participating in Transcriptional Activation, Cell Differentiation, and Malignant Transformation

ZC3H13-mediated N6-methyladenosine modification of PHF10 is impaired by fisetin which inhibits the DNA damage response in pancreatic cancer

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