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

DAM1 Dam1p

Dam1, Dam1p
Top mentioned proteins: Aurora, CAN, fibrillin-1, ASK1, Mps1
Papers on Dam1
The molecular architecture of the Dam1 kinetochore complex is defined by cross-linking based structural modelling.
Davis et al., Seattle, United States. In Nat Commun, 2014
Furthermore, the Dam1p amino terminus forms an interaction interface between Dam1 complexes, which is also disrupted by phosphorylation.
The signaling network that silences the spindle assembly checkpoint upon the establishment of chromosome bipolar attachment.
Wang et al., Tallahassee, United States. In Proc Natl Acad Sci U S A, 2014
Here we provide evidence indicating that Ipl1-dependent phosphorylation of the kinetochore protein Duo1 and Mps1 interacting (Dam1) prevents SAC silencing when tension is absent.
Iml3p, a component of the Ctf19 complex of the budding yeast kinetochore is required to maintain kinetochore integrity under conditions of spindle stress.
Ghosh et al., Calcutta, India. In Fems Yeast Res, 2013
Furthermore, in the absence of Iml3p, the two-hybrid interaction between Ctf19p (a member of the Ctf19 complex) and Dam1p (a member of the outer kinetochore DASH complex) was disrupted and the localization of Dam1p at the kinetochore was also compromised.
Phosphorylation of centromeric histone H3 variant regulates chromosome segregation in Saccharomyces cerevisiae.
Basrai et al., Bethesda, United States. In Mol Biol Cell, 2013
Consistent with these results, we observe that a phosphomimetic cse4-4SD mutant suppresses the temperature-sensitive growth of ipl1-2 and Ipl1 substrate mutants dam1 spc34 and ndc80, which are defective for chromosome biorientation.
Suppressors of ipl1-2 in components of a Glc7 phosphatase complex, Cdc48 AAA ATPase, TORC1, and the kinetochore.
Tatchell et al., Shreveport, United States. In G3 (bethesda), 2012
rev76 contains the missense mutation duo1-S115F, which alters an essential component of the DAM1/DASH complex.
Subunit organization in the Dam1 kinetochore complex and its ring around microtubules.
Nogales et al., Berkeley, United States. In Mol Biol Cell, 2011
The yeast Dam1 complex, an essential component of the outer kinetochore, forms rings around microtubules and in vitro recapitulates much of the functionality of a kinetochore-microtubule attachment.
Chromatin signaling to kinetochores: transregulation of Dam1 methylation by histone H2B ubiquitination.
Dent et al., Anderson, United States. In Cell, 2011
Paf1 complex and Rad6-Bre1-mediated ubiquitination of H2BK123 are required for Dam1 methylation at the kinetochore and therefore inhibit Ipl1-mediated phosphorylation, revealing unexpected functions for these proteins in mitosis.
The requirement for the Dam1 complex is dependent upon the number of kinetochore proteins and microtubules.
Berman et al., Minneapolis, United States. In Curr Biol, 2011
The Dam1 complex is required for viability because its function as a processivity factor for kinetochore-microtubule binding is more critical when chromosome segregation is dependent upon a single kinetochore-microtubule.
A piggyBac transposon-based mutagenesis system for the fission yeast Schizosaccharomyces pombe.
Du et al., Beijing, China. In Nucleic Acids Res, 2011
Using this system, we obtained loss-of-function alleles of klp5 and klp6, and a gain-of-function allele of dam1 from a screen for mutants resistant to the microtubule-destabilizing drug thiabendazole.
Laterally attached kinetochores recruit the checkpoint protein Bub1, but satisfy the spindle checkpoint.
Davis et al., Seattle, United States. In Cell Cycle, 2010
We have previously described a kinetochore mutant, DAM1-765, which exhibits lateral attachments and misregulation of microtubule length.
A non-ring-like form of the Dam1 complex modulates microtubule dynamics in fission yeast.
He et al., Houston, United States. In Proc Natl Acad Sci U S A, 2010
Fndings suggest that patches, instead of rings, are the physiologically functional forms of Dam1.
Cooperation of the Dam1 and Ndc80 kinetochore complexes enhances microtubule coupling and is regulated by aurora B.
Davis et al., Seattle, United States. In J Cell Biol, 2010
the interaction between the Ndc80 and Dam1 complexes is abolished when the Dam1 complex is phosphorylated by the yeast aurora B kinase Ipl1.
Conservation of the sterol regulatory element-binding protein pathway and its pathobiological importance in Cryptococcus neoformans.
Kwon-Chung et al., Bethesda, United States. In Eukaryot Cell, 2009
Furthermore, we show that C. neoformans contains an additional gene, DAM1, which functions in the SREBP pathway but is yet to be described.
Dormancy-associated MADS genes from the EVG locus of peach [Prunus persica (L.) Batsch] have distinct seasonal and photoperiodic expression patterns.
Bielenberg et al., United States. In J Exp Bot, 2008
DAM1, 2, 4, 5, and 6 were responsive to a reduction in photoperiod in controlled conditions and the direction of response correlated with the seasonal timing of expression in field-grown trees.
The Dam1 ring binds microtubules strongly enough to be a processive as well as energy-efficient coupler for chromosome motion.
Ataullakhanov et al., Boulder, United States. In Proc Natl Acad Sci U S A, 2008
Accurate chromosome segregation during mitotic division of budding yeast depends on the multiprotein kinetochore complex, Dam1 (also known as DASH).
Different assemblies of the DAM1 complex follow shortening microtubules by distinct mechanisms.
McIntosh et al., Boulder, United States. In Proc Natl Acad Sci U S A, 2008
Both rings and nonencircling Dam1 oligomers can track microtubule ends and enable processive cargo movement in vitro.
Fission yeast dam1-A8 mutant is resistant to and rescued by an anti-microtubule agent.
Toda et al., London, United Kingdom. In Biochem Biophys Res Commun, 2008
The Dam1/DASH outer kinetochore complex is required for high-fidelity chromosome segregation in budding and fission yeast.
Architecture of the Dam1 kinetochore ring complex and implications for microtubule-driven assembly and force-coupling mechanisms.
Nogales et al., Berkeley, United States. In Nat Struct Mol Biol, 2007
The architecture of the Dam1 complex at 30-A resolution and the self-assembly mechanism is defined.
Dam1 is the right one: phosphoregulation of kinetochore biorientation.
He et al., Houston, United States. In Dev Cell, 2002
Recent work has identified Dam1p, a member of the DASH complex, as the key Ipl1p substrate responsible for kinetochore/microtubule interaction.
Phospho-regulation of kinetochore-microtubule attachments by the Aurora kinase Ipl1p.
Barnes et al., Berkeley, United States. In Cell, 2002
Our systematic mutational analysis of the Ipl1p phosphorylation sites demonstrated that the essential microtubule binding protein Dam1p is a key Ipl1p target for regulating kinetochore-microtubule attachments in vivo.
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