The KASH protein Kms2 coordinates mitotic remodeling of the spindle pole body

Wälde, Sarah; King, Megan C.

doi:10.1242/jcs.154997

Cited by 35 publications

(43 citation statements)

References 93 publications

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“…Loss of Kms2 led to late mitotic entry, disruption of stable bipolar spindle formation, and abnormal insertion of the SPB. Interestingly, defects in recruitment of polo kinase, Plo1, to the SPB at mitotic entry were also observed in Kms2 deletion mutant cells (Walde and King, 2014), suggesting a role of Kms2-Sad1 in regulation of the SPB integration and mitotic entry.…”

Section: Functional Interactions Of the Linc Complexmentioning

confidence: 99%

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Making the LINC: SUN and KASH protein interactions

Kim

Birendra²,

Roux³

2015

Biological Chemistry

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Cell nuclei are physically integrated with the cytoskeleton through the LINC complex (for LInker of Nucleoskeleton and Cytoskeleton), a structure that spans the nuclear envelope to link the nucleoskeleton and cytoskeleton. Outer nuclear membrane KASH domain proteins and inner nuclear membrane SUN domain proteins interact to form the core of the LINC complex. In this review we provide a comprehensive analysis of the reported protein-protein interactions for KASH and SUN domain proteins. This critical structure, directly connecting the genome with the rest of the cell, contributes to a myriad of cellular functions and, when perturbed, is associated with human disease.

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Section: Functional Interactions Of the Linc Complexmentioning

confidence: 99%

“…Recently, core SPB components Cut12 and Pcp1 were identified as direct binding partners of Kms2 (Walde and King, 2014). Loss of Kms2 led to late mitotic entry, disruption of stable bipolar spindle formation, and abnormal insertion of the SPB.…”

Section: Functional Interactions Of the Linc Complexmentioning

confidence: 99%

Making the LINC: SUN and KASH protein interactions

Kim

Birendra²,

Roux³

2015

Biological Chemistry

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“…This work has focused on spindle length at steady state, not dynamic changes. However, some fission-yeast mutants exhibit large fluctuations in spindle length in which the bipolar spindle assembles, but then shortens or falls apart, known as spindle collapse [50,[52][53][54][55][56][57][58]. Re-markably, fission-yeast double mutants can have wild-type average metaphase spindle length, but much larger fluctuations than wild-type [50].…”

Section: Slow Turnover Of Kinetochore-microtubule Attachments Can Caumentioning

confidence: 99%

Mechanisms of chromosome biorientation and bipolar spindle assembly analyzed by computational modeling

Edelmaier

Lamson

Gergely

et al. 2019

Preprint

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The essential functions required for mitotic spindle assembly and chromosome biorientation and segregation are not fully understood, despite extensive study. To illuminate the combinations of ingredients most important to align and segregate chromosomes and simultaneously assemble a bipolar spindle, we developed a computational model of fission-yeast mitosis. Robust chromosome biorientation requires progressive restriction of attachment geometry, destabilization of misaligned attachments, and attachment force dependence. Large spindle length fluctuations can occur when the kinetochore-microtubule attachment lifetime is long. The primary spindle force generators are kinesin-5 motors and crosslinkers in early mitosis, while interkinetochore stretch becomes important after biorientation. The same mechanisms that contribute to persistent biorientation lead to segregation of chromosomes to the poles after anaphase onset. This model therefore provides a framework to interrogate key requirements for robust chromosome biorientation, spindle length regulation, and force generation in the spindle.

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“…The yeast strain MHY6952 (Sa-Moura et al 2013) was grown to mid-log phase (OD 600 = 0.5) in YPD (1% yeast extract, 2% peptone, 2% dextrose) at 30°C and harvested. The cell pellet was washed once with water, frozen in liquid nitrogen, and ground in a Retsch mill according to Wälde and King (2014). Approximately 100 μL of cryolysate of the yeast strain MHY6952 was rapidly thawed in 900 μL of 10% glycerol RNPB.…”

Section: Glycerol Gradient Sedimentation Analysismentioning

confidence: 99%

A protein interaction map of the LSU processome

et al. 2015

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Maturation of the large ribosomal subunit (LSU) in eukaryotes is a complex and highly coordinated process that requires the concerted action of a large, dynamic, ribonucleoprotein complex, the LSU processome. While we know that >80 ribosome biogenesis factors are required throughout the course of LSU assembly, little is known about how these factors interact with each other within the LSU processome. To interrogate its organization and architecture, we took a systems biology approach and performed a semi-high-throughput, array-based, directed yeast two-hybrid assay. Assaying 4800 protein-protein interactions, we identified 232 high-confidence, binary-interacting protein pairs, representing a fourfold increase from current knowledge. The resulting LSU processome interactome map has enhanced our understanding of the organization and function of the biogenesis factors within the LSU processome, revealing both novel and previously identified subcomplexes and hub proteins, including Nop4.[Keywords: LSU processome; RNA; ribosome; yeast two-hybrid] Supplemental material is available for this article. Eukaryotic ribosomes are complex cellular machines that are comprised of four different ribosomal RNAs (rRNAs) and >70 ribosomal proteins (r-proteins) (Woolford and Baserga 2013). Ribosome assembly begins in the nucleolus with the transcription of the polycistronic pre-rRNA, termed the 35S in Saccharomyces cerevisiae, by RNA polymerase I. The 35S pre-rRNA undergoes numerous cleavage and modification steps to generate the mature 18S, 5.8S, and 25S rRNAs that are assembled with the r-proteins to form the small and large ribosomal subunits. Accurate and efficient production of ribosomes requires the coordinated activity of >150 biogenesis factors, including a number of proteins with enzymatic activity (Fatica and Tollervey 2002; Fromont-Racine et al.

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The KASH protein Kms2 coordinates mitotic remodeling of the spindle pole body

Cited by 35 publications

References 93 publications

Making the LINC: SUN and KASH protein interactions

Making the LINC: SUN and KASH protein interactions

Mechanisms of chromosome biorientation and bipolar spindle assembly analyzed by computational modeling

A protein interaction map of the LSU processome

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