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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 24 Oct 2014.

MLF1 interacting protein

MLF1IP, MLF1-interacting protein, PBIP1, CENP-50, CENP-U, KLIP1
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). MLF1IP, or CENPU, is an additional factor required for centromere assembly (Foltz et al., 2006 [PubMed 16622419]).[supplied by OMIM, Mar 2008] (from NCBI)
Top mentioned proteins: MLF1, Plk1, CENP-Q, Gli, NRIF3
Papers on MLF1IP
The CENP-O complex requirement varies among different cell types.
New
Fukagawa et al., Mishima, Japan. In Chromosome Res, 30 Sep 2014
CENP-U (CENP-50) is a component of the CENP-O complex, which includes CENP-O, CENP-P, CENP-Q, CENP-R, and CENP-U and is constitutively localized at kinetochores throughout the cell cycle in vertebrates.
A cooperative mechanism drives budding yeast kinetochore assembly downstream of CENP-A.
New
Westermann et al., Vienna, Austria. In J Cell Biol, 18 Sep 2014
We show that the conserved kinetochore subunits Ame1(CENP-U) and Okp1(CENP-Q) form a DNA-binding complex that associates with the microtubule-binding KMN network via a short Mtw1 recruitment motif in the N terminus of Ame1.
Subcellular localization of full-length human myeloid leukemia factor 1 (MLF1) is independent of 14-3-3 proteins.
New
Ottmann et al., Dortmund, Germany. In Cell Mol Biol Lett, Mar 2013
However, information on the physiological function of MLF1 is limited and mostly derived from studies identifying MLF1 interaction partners like CSN3, MLF1IP, MADM, Manp and the 14-3-3 proteins.
The ABCs of CENPs.
Review
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.
Mammalian polo-like kinase 1-dependent regulation of the PBIP1-CENP-Q complex at kinetochores.
GeneRIF
Lee et al., Bethesda, United States. In J Biol Chem, 2011
Mammalian polo-like kinase 1-dependent regulation of the PBIP1-CENP-Q complex at kinetochores.
Feed-forward mechanism of converting biochemical cooperativity to mitotic processes at the kinetochore plate.
Lee et al., Bethesda, United States. In Proc Natl Acad Sci U S A, 2011
Using a pair of ELISA, here we demonstrated that mutations of the self-priming site of a kinetochore component, PBIP1/MLF1IP/KLIP1/CENP-50/CENP-U (PBIP1), to a Cdk1-dependent non-self-priming site abolished product-activated cooperativity in the formation of the Plk1-PBIP1 complex.
CENP-U cooperates with Hec1 to orchestrate kinetochore-microtubule attachment.
GeneRIF
Yao et al., Hefei, China. In J Biol Chem, 2011
CENP-U is a novel microtubule binding protein and plays an important role in kinetochore-microtubule attachment through its interaction with Hec1
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.
Acceptor-photobleaching FRET analysis of core kinetochore and NAC proteins in living human cells.
Diekmann et al., Jena, Germany. In Eur Biophys J, 2009
The data indicate that CENP-U is in close vicinity to CENP-I as well as to CENP-B and that CENP-M is close to CENP-T.
CENP-O class proteins form a stable complex and are required for proper kinetochore function.
Fukagawa et al., Mishima, Japan. In Mol Biol Cell, 2008
Phenotype analysis of knockout cells showed that all proteins except for CENP-R were required for recovery from spindle damage, and phosphorylation of CENP-50 was essential for recovery from spindle damage.
Self-regulated mechanism of Plk1 localization to kinetochores: lessons from the Plk1-PBIP1 interaction.
Park et al., Bethesda, United States. In Cell Div, 2007
Recent progress in our understanding of Plk1 localization to the centromeres shows that Plk1 self-regulates its initial recruitment by phosphorylating a centromeric component PBIP1 and generating its own PBD-binding site.
MLF1-interacting protein is mainly localized in nucleolus through N-terminal bipartite nuclear localization signal.
GeneRIF
Horiguchi-Yamada et al., Tokyo, Japan. In Anticancer Res, 2007
Deletion mutants of MLF1IP revealed that the N-terminal bipartite nuclear localization signal (NLS) was responsible for nucleolar targeting.
Grabbing Plk1 by the PBD.
Review
Wang et al., New York City, United States. In Mol Cell, 2006
A new centromeric protein termed PBIP1 was identified that recruits Plk1 to the kinetochores.
Self-regulated Plk1 recruitment to kinetochores by the Plk1-PBIP1 interaction is critical for proper chromosome segregation.
GeneRIF
Lee et al., Bethesda, United States. In Mol Cell, 2006
Plk1 self-regulates the Plk1-PBIP1 interaction to timely localize to the kinetochores and promote proper chromosome segregation.
The human CENP-A centromeric nucleosome-associated complex.
Impact
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.
Cloning of a newly identified heart-specific troponin I isoform, which lacks the troponin T binding portion, using the yeast hybrid system.
Horiguchi-Yamada et al., In Exp Clin Cardiol, 2005
METHODS: Yeast two-hybrid screen analysis was performed using MLF1-interacting protein (amino acids 1 to 318) as bait.
Regulation of myeloid leukemia factor-1 interacting protein (MLF1IP) expression in glioblastoma.
GeneRIF
Robertson et al., Memphis, United States. In Brain Res, 2005
MLF1IP was found in glioblastomas where it was co-localized with MLF1 and nestin. Moreover, it was elevated in the contralateral brain where no tumor cells occurred, suggesting a role in glioma pathogenesis and potentially in other types of malignancies.
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