Looping in on Ndc80 – How does a protein loop at the kinetochore control chromosome segregation?

Nilsson, Jakob

doi:10.1002/bies.201200096

Cited by 17 publications

(18 citation statements)

References 103 publications

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“…This loop was suggested to play a structural role in kinetochore geometry and/or the tension-sensing mechanism, yet its precise function at the molecular level remained elusive for some time [6]. Recent studies from several laboratories have started to uncover its precise role [7,8]. …”

Section: Main Text and Discussionmentioning

confidence: 99%

Ndc80 Loop as a protein-protein interaction motif

Tang

Toda

2013

Cell Div

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Our understanding of the structure and function of kinetochores has advanced dramatically over the past 10 years, yet how the plus end of spindle microtubules interacts with the kinetochore and establishes amphitelic attachment for proper sister chromatid segregation remains unresolved. However, several recent reports from different organisms have shed new light on this issue. A key player in microtubule-kinetochore interaction is the conserved Ndc80 outer kinetochore complex. In both yeast and human cells in particular, a ubiquitous internal ‘loop’ found in the Ndc80 molecule interrupting its C-terminal coiled-coil domain plays critical roles in protein-protein interaction, by recruiting microtubule-binding proteins to ensure proper kinetochore-microtubule attachment. In this commentary, we summarise the recent progress made and discuss the evolutionary significance of this loop’s role in microtubule dynamics at the kinetochore for accurate chromosome segregation.

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Section: Main Text and Discussionmentioning

confidence: 99%

Ndc80 Loop as a protein-protein interaction motif

Tang

Toda

2013

Cell Div

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“…After the acceptance of this manuscript, a review written by Jakob Nilsson was published in the journal Bioessays, describing in detailed the function of the Ndc80 loop domain (Nilsson, 2012).…”

Section: Acknowledgementsmentioning

confidence: 99%

The KMN protein network – chief conductors of the kinetochore orchestra

Varma

Salmon

2012

Journal of Cell Science

118

108

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SummarySuccessful completion of mitosis requires that sister kinetochores become attached end-on to the plus ends of spindle microtubules (MTs) in prometaphase, thereby forming kinetochore microtubules (kMTs) that tether one sister to one spindle pole and the other sister to the opposite pole. Sites for kMT attachment provide at least four key functions: robust and dynamic kMT anchorage; force generation that can be coupled to kMT plus-end dynamics; correction of errors in kMT attachment; and control of the spindle assembly checkpoint (SAC). The SAC typically delays anaphase until chromosomes achieve metaphase alignment with each sister kinetochore acquiring a full complement of kMTs. Although it has been known for over 30 years that MT motor proteins reside at kinetochores, a highly conserved network of protein complexes, called the KMN network, has emerged in recent years as the primary interface between the kinetochore and kMTs. This Commentary will summarize recent advances in our understanding of the role of the KMN network for the key kinetochore functions, with a focus on human cells.

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“…Although this loop may play a structural role, such as in the introduction of the coiled-coil kink to the rod region of the Ndc80 complex (Wang et al ., 2008; Wan et al ., 2009; Varma et al ., 2012; Zhang et al ., 2012), most recent results from yeasts and humans have shown that this domain also acts as a protein–protein interaction motif (Hsu and Toda, 2011; Tang and Toda, 2013; Maure et al ., 2011; Nilsson, 2012; Varma et al ., 2012; Varma and Salmon, 2012; Zhang et al ., 2012). We previously showed that the Ndc80 loop in fission yeast recruits the Dis1 microtubule-associated protein (Ohkura et al ., 1988; Nabeshima et al ., 1995) to the mitotic outer kinetochore via direct interaction (Hsu and Toda, 2011).…”

Section: Introductionmentioning

confidence: 99%