The Vertebrate Ndc80 Complex Contains Spc24 and Spc25 Homologs, which Are Required to Establish and Maintain Kinetochore-Microtubule Attachment
Mark L. McCleland,Marko J. Kallio,Gregory A. Barrett-Wilt,Cortney A. Kestner,Jeffrey Shabanowitz,Donald F. Hunt,Gary J. Gorbsky,P. Todd Stukenberg +7 more
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TLDR
Previous characterization of the Ndc80/Hec1 kinetochore complex is extended and it is found that Spc24 and Spc25 are required not only to establish, but also to maintain kinetchore-microtubule attachments and metaphase alignment.About:
This article is published in Current Biology.The article was published on 2004-01-20 and is currently open access. It has received 172 citations till now. The article focuses on the topics: Ndc80 complex & Kinetochore.read more
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The Conserved KMN Network Constitutes the Core Microtubule-Binding Site of the Kinetochore
TL;DR: It is proposed that the conserved KNL-1/Mis12 complex/Ndc80 complex (KMN) network constitutes the core microtubule-binding site of the kinetochore.
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Kinetochore microtubule dynamics and attachment stability are regulated by Hec1.
Jennifer G. DeLuca,Walter E. Gall,Claudio Ciferri,Daniela Cimini,Andrea Musacchio,Edward D. Salmon +5 more
TL;DR: It is reported here that Ndc80/Hec1 functions in regulating kinetochore microtubule plus-end dynamics and attachment stability, and a key role for the Hec1 N terminus is revealed in controlling dynamic behavior of kinetic microtubules.
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Implications for Kinetochore-Microtubule Attachment from the Structure of an Engineered Ndc80 Complex
Claudio Ciferri,Sebastiano Pasqualato,Emanuela Screpanti,Gianluca Varetti,Stefano Santaguida,Gabriel Dos Reis,Alessio Maiolica,Jessica K. Polka,Jennifer G. De Luca,Peter De Wulf,Mogjiborahman Salek,Juri Rappsilber,Carolyn A. Moores,Edward D. Salmon,Andrea Musacchio +14 more
TL;DR: An engineered "bonsai" Ndc80 complex containing a shortened rod domain but retaining the globular domains required for kinetochore localization and microtubule binding is crystallized, revealing a microtubules-binding interface containing a pair of tightly interacting calponin-homology (CH) domains with a previously unknown arrangement.
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A conserved protein network controls assembly of the outer kinetochore and its ability to sustain tension
Iain M. Cheeseman,Sherry Niessen,Scott Anderson,Francie Hyndman,John R. Yates,Karen Oegema,Arshad Desai +6 more
TL;DR: A set of 10 copurifying kinetochore proteins from Caenorhabditis elegans are identified, seven of which were previously uncharacterized, and it is shown that thisCopurifying protein network plays a central role at the kinetchore-microtubule interface.
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The dynamic kinetochore-microtubule interface.
TL;DR: The kinetochore is a control module that both powers and regulates chromosome segregation in mitosis and meiosis, and recent work has revealed that many kinetchore components are highly dynamic and that some cycle between Kinetochores and spindle poles along microtubules.
References
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TL;DR: This method was used to delineate coiled-coil domains in otherwise globular proteins, such as the leucine zipper domains in transcriptional regulators, and to predict regions of discontinuity within coiled -coil structures,such as the hinge region in myosin.
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Centromeres and Kinetochores: From Epigenetics to Mitotic Checkpoint Signaling
TL;DR: Efforts to understand the nature and specification of the centromere have demonstrated that this central element for ensuring inheritance is itself epigenetically determined.
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Role of Hec1 in Spindle Checkpoint Signaling and Kinetochore Recruitment of Mad1/Mad2
TL;DR: The spindle checkpoint delays sister chromatid separation until all chromosomes have undergone bipolar spindle attachment and it was shown that the human protein Hec1 was required for the recruitment of Mps1 kinase and Mad1/Mad2 complexes to kinetochores.
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The Ndc80p complex from Saccharomyces cerevisiae contains conserved centromere components and has a function in chromosome segregation.
TL;DR: The Ndc80p complex contains centromere-associated components conserved between yeasts and vertebrates and is purified from Saccharomyces cerevisiae.
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Analysis of the Saccharomyces Spindle Pole by Matrix-assisted Laser Desorption/Ionization (MALDI) Mass Spectrometry
TL;DR: This is the first report of the identification of the components of a large cellular organelle by MALDI peptide mapping alone.