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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Centromere protein N

The centromere is a specialized chromatin domain, present throughout the cell cycle, that acts as a platform on which the transient assembly of the kinetochore occurs during mitosis. All active centromeres are characterized by the presence of long arrays of nucleosomes in which CENPA (MIM 117139) replaces histone H3 (see MIM 601128). CENPN is an additional factor required for centromere assembly (Foltz et al., 2006 [PubMed 16622419]).[supplied by OMIM, Mar 2008] (from NCBI)
Top mentioned proteins: Gli, Histone, CENP-H, CENP-C, Mis6
Papers on CENP-N
A supergene determines highly divergent male reproductive morphs in the ruff.
Burke et al., Graz, Austria. In Nat Genet, Jan 2016
One breakpoint of the inversion disrupts the essential CENP-N gene (encoding centromere protein N), and pedigree analysis confirms the lethality of homozygosity for the inversion.
Whole-proteome genetic analysis of dependencies in assembly of a vertebrate kinetochore.
Earnshaw et al., Suita, Japan. In J Cell Biol, Jan 2016
Surprisingly, CENP-T depends on CENP-N for chromosome localization.
Structural transitions of centromeric chromatin regulate the cell cycle-dependent recruitment of CENP-N.
Li et al., Beijing, China. In Genes Dev, Jun 2015
Specific recognition of centromere-specific histone variant CENP-A-containing chromatin by CENP-N is an essential process in the assembly of the kinetochore complex at centromeres prior to mammalian cell division.
Structural insights into the role of the Chl4-Iml3 complex in kinetochore assembly.
Li et al., Hefei, China. In Acta Crystallogr D Biol Crystallogr, 2013
Human CENP-N and CENP-L have been reported to selectively recognize the CENP-A nucleosome and to contribute to recruiting other constitutive centromere-associated network (CCAN) complexes involved in assembly of the inner kinetochore.
An Iml3-Chl4 heterodimer links the core centromere to factors required for accurate chromosome segregation.
Harrison et al., Boston, United States. In Cell Rep, 2013
Proteins recruited by Chl4/CENP-N include a subset that regulates chromosome transmission fidelity.
Step-wise assembly, maturation and dynamic behavior of the human CENP-P/O/R/Q/U kinetochore sub-complex.
Diekmann et al., Jena, Germany. In Plos One, 2011
Furthermore, CENP-P/O/R/Q/U binding to the CCAN is largely mediated through interactions with the CENP-N binding protein CENP-L as well as CENP-K.
Dynamics of CENP-N kinetochore binding during the cell cycle.
Diekmann et al., Jena, Germany. In J Cell Sci, 2011
CENP-N is bound to kinetochores during S phase and G2, but is absent from kinetochores during mitosis and G1.
The ABCs of CENPs.
Fukagawa et al., Mishima, Japan. In Chromosoma, 2011
Onto centromeric CENP-A chromatin is assembled the so-called constitutive centromere-associated network (CCAN) of 16 proteins distributed in several functional groups as follows: CENP-C, CENP-H/CENP-I/CENP-K/, CENP-L/CENP-M/CENP-N, CENP-O/CENP-P/CENP-Q/CENP-R/CENP-U(50), CENP-T/CENP-W, and CENP-S/CENP-X.
Dual recognition of CENP-A nucleosomes is required for centromere assembly.
Straight et al., Palo Alto, United States. In J Cell Biol, 2010
We previously identified CENP-N as a CENP-A nucleosome-specific binding protein.
A super-resolution map of the vertebrate kinetochore.
Earnshaw et al., Edinburgh, United Kingdom. In Proc Natl Acad Sci U S A, 2010
Loss of CENP-H, CENP-N, or CENP-W had little or no effect on the unfolding of mitotic kinetochores.
Double-strand DNA breaks recruit the centromeric histone CENP-A.
Cleveland et al., San Diego, United States. In Proc Natl Acad Sci U S A, 2009
Using multiphoton absorption and DNA cleavage at unique sites by I-SceI endonuclease, we demonstrate that CENP-A is rapidly recruited to double-strand breaks in DNA, along with three components (CENP-N, CENP-T, and CENP-U) associated with CENP-A at centromeres.
A reader for centromeric chromatin.
Black et al., In Nat Cell Biol, 2009
CENP-N has now been identified as a reader of the centromere-specifying epigenetic mark that is generated by incorporation of the histone H3 variant CENP-A into centromeric nucleosomes.
Centromere assembly requires the direct recognition of CENP-A nucleosomes by CENP-N.
Straight et al., Palo Alto, United States. In Nat Cell Biol, 2009
Data suggest that CENP-N interprets the information encoded within CENP-A nucleosomes and recruits other proteins to centromeric chromatin that are required for centromere function and propagation.
The CENP-A NAC/CAD kinetochore complex controls chromosome congression and spindle bipolarity.
Meraldi et al., Maglie, Italy. In Embo J, 2008
In contrast, depletion of Class II proteins (CENP-H, Chl4R(CENP-N), CENP-I and Sim4R(CENP-K)) prevents binding of Class I proteins and causes chromosome congression defects, but does not perturb spindle formation.
The human CENP-A centromeric nucleosome-associated complex.
Cleveland et al., San Diego, United States. In Nat Cell Biol, 2006
Here, we show that CENP-A nucleosomes directly recruit a proximal CENP-A nucleosome associated complex (NAC) comprised of three new human centromere proteins (CENP-M, CENP-N and CENP-T), along with CENP-U(50), CENP-C and CENP-H.
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