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CENP-A undergoes alpha-amino trimethylation by the enzyme NRMT (show METTL11A Proteins) in vivo.
H4K5ac and H4K12ac, mediated by RbAp46 (show RBBP7 Proteins)/48, facilitates efficient CENP-A deposition into centromeres.
Collectively, these studies clarify how CENP-N (show CENPN Proteins) and CENP-C decode and stabilize the non-canonical CENP-A nucleosome to enforce epigenetic centromere specification and kinetochore assembly.
the SGT1 (show SUGT1 Proteins)-HSP90 (show HSP90 Proteins) complex contributes to the E3 ligase activity of the CUL4A (show CUL4A Proteins) complex that is necessary for CENP-A ubiquitylation and CENP-A deposition at the centromere.
during the CENP-A/H4 deposition process, the chaperone HJURP (show HJURP Proteins) protects various substructures of the dimer, serving both as a folding and binding chaperone
This study provides insights into how overexpression of CENP-A may contribute to CIN (show PDXP Proteins) in cancers and underscore the importance of understanding the pathways that prevent CENP-A mislocalization for genome stability.
Findings indicate the role of the amino-terminus of centromere protein A (CENP-A) in localization.
Levels of centromere aberrations increase upon depletion of CENP-A, CENP-C, and CENP-T (show CENPT Proteins)/W, during replicative senescence, and in cancer cells.
findings demonstrate the involvement of consensus Cdk1 (show CDK1 Proteins) phosphorylation sites on Mis18 complex assembly and thus provide a rationale for cell cycle-regulated timing of Mis18 assembly and CENP-A deposition
Upon cross-linking, the entire CENPA/CENPB (show CENPB Proteins)/CENPC/CENPT (show CENPT Proteins) complex is nuclease (show DCLRE1C Proteins)-protected over an alpha-satellite dimer that comprises the fundamental unit of centromeric chromatin. We conclude that CENPA/CENPC and CENPT (show CENPT Proteins) pathways for kinetochore assembly are physically integrated over young alpha-satellite dimers.
Centromeres with more satellite repeats house more nucleosomes that confer centromere identity, containing the histone H3 (show HIST3H3 Proteins) variant CENP-A, and bias their segregation to the egg relative to centromeres with fewer repeats.
The findings provide evidence that CENP-A is critical for the faithful chromosome segregation during mammalian oocyte meiosis.
evolutionarily conserved flexible ends of the CENP-A nucleosomes are essential to ensure the fidelity of the mitotic pathway.
These data implicate the insulin (show INS Proteins)-FoxM1 (show FOXM1 Proteins)/PLK1/CENP-A pathway-regulated mitotic cell-cycle progression as an essential component in the beta cell adaptation to delay and/or prevent progression to diabetes.
CPCs maintain relatively high levels of CENP-A early in life, which is necessary for sustaining proliferation, inhibiting senescence, and promoting survival following differentiation of CPCs.
Results report that the level of CENP-A, a protein required for cell division, declines precipitously with age in an islet-specific manner.
Cenpa, Cenpb (show CENPB Proteins), and Bub3 (show BUB3 Proteins), but not Cenpc, interacted with PARP-1 (show PARP1 Proteins)
The centromere-targeting domain of CENP-A is both necessary and sufficient for recruitment to double-strand breaks. CENP-A accumulation at DNA breaks is enhanced by active non-homologous end-joining but does not require DNA-PKcs (show PRKDC Proteins) or Ligase IV.
CENP-C and M18BP1 (show MIS18BP1 Proteins) recruit HJURP (show HJURP Proteins) to centromeres for new CENP-A assembly.
CENP-A assembly into chromatin requires unidentified deoxycytidine deaminase (show APOBEC3G Proteins) and UNG2 (show CCNO Proteins), a uracil DNA glycosylase (show UNG Proteins).
CENP-A deposition at the centromeres is dependent on HJURP (show HJURP Proteins).
Centromeres are the differentiated chromosomal domains that specify the mitotic behavior of chromosomes. CENPA encodes a centromere protein which contains a histone H3 related histone fold domain that is required for targeting to the centromere. CENPA is proposed to be a component of a modified nucleosome or nucleosome-like structure in which it replaces 1 or both copies of conventional histone H3 in the (H3-H4)2 tetrameric core of the nucleosome particle. Alternative splicing results in multiple transcript variants encoding distinct isoforms.
centromere autoantigen A
, centromere protein A, 17kDa
, centromere-specific histone
, histone H3-like centromeric protein A
, centrosomin A
, centromere protein, Xenopus
, centromeric histone-3 like protein
, centromere protein A