"MYSM1 is Involved in Maintaining Genome Stability and histone Ubiquitylation
MYSM1 is a member of
the MPN+/JAMM family of DUBs. It was initially identified as a
histone H2A deubiquitylating enzyme involved in regulating
transcriptional programmes and epigenetic regulation of B cell
differentiation [152,
153].
Furthermore,
analyses of MYSM1 deficient mice uncovered a role for MYSM1 in bone
marrow stem cell maintenance, control of oxidative stress and genomic
stability in hematopoietic progenitors, and in the development of
lymphoid and erythroid lineages [154].
Given the intricate
links between epigenetic regulation of histone ubiquitylation and DNA
damage responses [13],
it will be interesting to further explore the roles played by MYSM1
in such processes"
https://core.ac.uk/download/pdf/82824728.pdf
https://core.ac.uk/download/pdf/82824728.pdf
Tapaan toisen kerran
MYSM1- proteiinin 15.6. 2019, kun seulon geeniryhmää ”BMFS”
numero numerolta, BMFS1,-2,-3,-4,-5.
BMFS4 on MYSM1.
Lisätietoa:
https://www.cell.com/molecular-cell/fulltext/S1097-2765(07)00516-3?_returnURL=https%3A%2F%2Flinkinghub.elsevier.com%2Fretrieve%2Fpii%2FS1097276507005163%3Fshowall%3Dtrue
Lisätietoa:
https://www.cell.com/molecular-cell/fulltext/S1097-2765(07)00516-3?_returnURL=https%3A%2F%2Flinkinghub.elsevier.com%2Fretrieve%2Fpii%2FS1097276507005163%3Fshowall%3Dtrue
A Histone H2A Deubiquitinase Complex Coordinating Histone Acetylation
and H1 Dissociation in Transcriptional Regulation
Summary
Deciphering
the epigenetic “code” remains a central issue in transcriptional
regulation. Here, we report the identification of a JAMM/MPN+ domain-containing histone H2A deubiquitinase
(2A-DUB, or KIAA1915/MYSM1) specific for monoubiquitinated H2A (uH2A)
that has permitted delineation of a strategy for specific regulatory
pathways of gene activation. 2A-DUB regulates transcription by
coordinating histone acetylation and deubiquitination, and destabilizing
the association of linker histone H1 with nucleosomes.
2A-DUB interacts with p/CAF in a coregulatory protein complex, with its deubiquitinase activity modulated by the status of acetylation of nucleosomal histones. Consistent with this mechanistic role, 2A-DUB participates in transcriptional regulation events in androgen receptor-dependent gene activation, and the levels of uH2A are dramatically decreased in prostate tumors, serving as a cancer-related mark. We suggest that H2A ubiquitination represents a widely used mechanism for many regulatory transcriptional programs and predict that various H2A ubiquitin ligases/deubiquitinases will be identified for specific cohorts of regulated transcription units.
2A-DUB interacts with p/CAF in a coregulatory protein complex, with its deubiquitinase activity modulated by the status of acetylation of nucleosomal histones. Consistent with this mechanistic role, 2A-DUB participates in transcriptional regulation events in androgen receptor-dependent gene activation, and the levels of uH2A are dramatically decreased in prostate tumors, serving as a cancer-related mark. We suggest that H2A ubiquitination represents a widely used mechanism for many regulatory transcriptional programs and predict that various H2A ubiquitin ligases/deubiquitinases will be identified for specific cohorts of regulated transcription units.
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