Formation of a Dynamic Kinetochore- Microtubule Interface through Assembly of the Dam1 Ring Complex

Westermann, Stefan; Avila-Sakar, Agustin; Wang, Hongwei; Niederstrasser, Hanspeter; Wong, Jonathan; Drubin, David G.; Nogales, Eva; Barnes, Georjana

doi:10.1016/j.molcel.2004.12.019

Cited by 288 publications

(434 citation statements)

References 35 publications

Supporting

Mentioning

406

Contrasting

Unclassified

Order By: Relevance

“…In addition, the DASH complex is localized at the kinetochore and the spindle and is required for spindle attachment to the kinetochore (Cheeseman et al, 2001;Li et al, 2002). The S. cerevisiae DASH complex is composed of 10 proteins that localize at the kinetochore and the spindle (Miranda et al, 2005;Westermann et al, 2005). Biochemical analyses have revealed that the kinetochore complex is comprised of subcomplexes of proteins.…”

Section: Introductionmentioning

confidence: 99%

Reconstruction of the Kinetochore during Meiosis in Fission Yeast Schizosaccharomyces pombe

Hayashi

Asakawa

Haraguchi

et al. 2006

MBoC

View full text Add to dashboard Cite

During the transition from mitosis to meiosis, the kinetochore undergoes significant reorganization, switching from a bipolar to a monopolar orientation. To examine the centromere proteins that are involved in fundamental reorganization in meiosis, we observed the localization of 22 mitotic and 2 meiotic protein components of the kinetochore during meiosis in living cells of the fission yeast. We found that the 22 mitotic proteins can be classified into three groups: the Mis6-like group, the NMS (Ndc80-Mis12-Spc7) group, and the DASH group, based on their meiotic behavior. Mis6-like group proteins remain at the centromere throughout meiosis. NMS group proteins disappear from the centromere at the onset of meiosis and reappear at the centromere in two steps in late prophase. DASH group proteins appear shortly before metaphase of meiosis I. These observations suggest that Mis6-like group proteins constitute the structural basis of the centromere and that the NMS and DASH group proteins reassemble to establish the functional metaphase kinetochore. On the other hand, the meiosis-specific protein Moa1, which plays an important role in forming the meiotic monopolar kinetochore, is loaded onto the centromere significantly earlier than the NMS group, whereas another meiosis-specific protein, Sgo1, is loaded at times similar to the NMS group.

show abstract

Section: Introductionmentioning

confidence: 99%

Reconstruction of the Kinetochore during Meiosis in Fission Yeast Schizosaccharomyces pombe

Hayashi

Asakawa

Haraguchi

et al. 2006

MBoC

View full text Add to dashboard Cite

show abstract

“…To overcome these limitations, we relied on a motility assay using the Dam1 complex 11 (also known as DASH, or DDD), a putative load-bearing component of kinetochores in yeast [11][12][13][14]26 . Like kinetochores, pure recombinant Dam1 complex forms robust connections to growing and shortening MT tips that remain attached even when tension is applied 14 .…”

mentioning

confidence: 99%

Tension applied through the Dam1 complex promotes microtubule elongation providing a direct mechanism for length control in mitosis

et al. 2007

View full text Add to dashboard Cite

In dividing cells, kinetochores couple chromosomes to the tips of growing and shortening microtubule (MT) fibers 1, 2 and tension at the kinetochore-MT interface promotes fiber elongation 3-6 . Tension-dependent MT fiber elongation is thought to be essential for coordinating chromosome alignment and separation 1, 3, 7-10 , but the mechanism underlying this effect is unknown. Using optical tweezers, we applied tension to a model of the kinetochore-microtubule interface composed of the yeast Dam1 complex 11-13 bound to individual dynamic microtubule tips 14 . Higher tension decreased the likelihood that growing tips would begin to shorten, slowed shortening, and increased the likelihood that shortening tips would resume growth. These effects are similar to the effects of tension on kinetochore-attached microtubule fibers in many cell types, suggesting that we have reconstituted a direct mechanism for microtubule length control in mitosis.For decades, a central problem for biologists has been to understand how MT lengths are controlled during mitosis 15, 16 . MTs are protein polymers that switch stochastically between phases of assembly and disassembly, during which tubulin subunits are added or lost from the filament tips 1 . This behavior, called 'dynamic instability', can be described by four parameters: the speeds of growth and shortening, and the rates of switching from growth to shortening and from shortening to growth, transitions known as 'catastrophes ' and 'rescues' 1, 17 In dividing cells, chromosomes are linked to the tips of MT fibers through specialized structures called kinetochores and their movements are coupled to fiber growth and shortening 1, 2 . Remarkably, kinetochores maintain persistent, load-bearing attachments to microtubule tips even as the filaments assemble and disassemble under their grip 1, 2, 18 . Classic micromanipulation experiments show that tension at the kinetochore-MT interface promotes MT fiber elongation 3-6 , and this effect is widely believed to be essential for controlling fiber lengths and thereby coordinating chromosome alignment and separation 1, 3, 7-10, 16 . Very little is known about the mechanism underlying this tension-dependent length control. However, the dynamic behavior of kinetochore-attached MT tips 18 implies that the mechanism underlying tension-dependent length control in vivo may act by altering one or more of the parameters of dynamic instability in response to load.A key unanswered question is whether tension promotes elongation via an indirect mechanism, where force transmitted through load-bearing kinetochore components regulates the activity of separate MT-modifying components, or by a direct mechanism, where the load-bearing Correspondence should be addressed to C.L.A.. * These authors contributed equally to this work. NIH Public Access Author ManuscriptNat Cell Biol. Author manuscript; available in PMC 2009 May 13. Published in final edited form as:Nat Cell Biol. 2007 July ; 9(7): 832-837. doi:10.1038/ncb1609. NIH-PA Author ManuscriptNIH-P...

show abstract

“…Another important candidate found in budding yeast was the Dam1 complex, which can form rings around microtubules in vitro [129].…”

Section: Force Generation By Microtubule Depolymerization From Plus-endsmentioning

confidence: 99%

The perpetual movements of anaphase

Maiato

Lince-Faria

2010

Cell. Mol. Life Sci.

View full text Add to dashboard Cite

One of the most extraordinary events in the lifetime of a cell is the coordinated separation of sister chromatids during cell division. This is truly the essence of the entire mitotic process and the reason for the most profound morphological changes in cytoskeleton and nuclear organization that a cell may ever experience. It all occurs within a very short time window known as "anaphase", as if the cell had spent the rest of its existence getting ready for this moment in an ultimate act of survival. And there is a good reason for this: no space for mistakes. Problems in the distribution of chromosomes during cell division have been correlated with aneuploidy, a common feature observed in cancers and several birth defects, and the main cause of spontaneous abortion in humans. In this paper we critically review the mechanisms of anaphase chromosome motion that resisted the scrutiny of more than one hundred years of research as part of a tribute to the pioneering work of Miguel Mota.

show abstract

Formation of a Dynamic Kinetochore- Microtubule Interface through Assembly of the Dam1 Ring Complex

Cited by 288 publications

References 35 publications

Reconstruction of the Kinetochore during Meiosis in Fission Yeast Schizosaccharomyces pombe

Reconstruction of the Kinetochore during Meiosis in Fission Yeast Schizosaccharomyces pombe

Tension applied through the Dam1 complex promotes microtubule elongation providing a direct mechanism for length control in mitosis

The perpetual movements of anaphase

Contact Info

Product

Resources

About