Kar3 interaction with Cik1 alters motor structure and function

Chu, Hsiao Mei Annie; Yun, Mikyung; Anderson, David E.; Sage, Harvey J.; Park, Hee-Won; Endow, Sharyn A.

doi:10.1038/sj.emboj.7600790

Cited by 35 publications

(36 citation statements)

References 34 publications

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“…studies suggest that members of the Kinesin-14 family actually possess the ability to destabilize rather than to stabilize MTs (Endow et al, 1994b;Chu et al, 2005;Sproul et al, 2005). Our data showed that in human cells and in Xenopus extracts Kinesin-14 proteins promote the outward movement of the spindle poles and increase half spindle length in monopolar spindles (data not shown).…”

Section: Kinesin-14s Affect Spindle Length Through Mt Slidingmentioning

confidence: 48%

Kinesin-14 Family Proteins HSET/XCTK2 Control Spindle Length by Cross-Linking and Sliding Microtubules

Cai

Weaver

Ems-McClung

et al. 2009

MBoC

175

201

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Kinesin-14 family proteins are minus-end directed motors that cross-link microtubules and play key roles during spindle assembly. We showed previously that the Xenopus Kinesin-14 XCTK2 is regulated by Ran via the association of a bipartite NLS in the tail of XCTK2 with importin ␣/␤, which regulates its ability to cross-link microtubules during spindle formation. Here we show that mutation of the nuclear localization signal (

show abstract

Section: Kinesin-14s Affect Spindle Length Through Mt Slidingmentioning

confidence: 48%

Kinesin-14 Family Proteins HSET/XCTK2 Control Spindle Length by Cross-Linking and Sliding Microtubules

Cai

Weaver

Ems-McClung

et al. 2009

MBoC

175

201

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show abstract

“…However, diverse cellular processes such as transcription, mRNA processing, spindle dynamics, and sister chromatid cohesion were also represented within the intersection dataset. Interestingly, tolerance to HU requires KAR3 and CIK1, which encode proteins that physically interact to form a minus-enddirected kinesin (Chu et al, 2005;Sproul et al, 2005), consistent with recent studies that implicate Mec1 and Rad53 in the regulation of spindle dynamics (Krishnan et al, 2004;Bachant et al, 2005). These genome-wide screens reveal that resistance to replication stress engages diverse cell regulatory processes.…”

Section: B=63mentioning

confidence: 48%

Ccr4 contributes to tolerance of replication stress through control ofCRT1mRNA poly(A) tail length

Woolstencroft

Cook

Preiß

et al. 2006

Journal of Cell Science

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In Saccharomyces cerevisiae, DNA replication stress activates the replication checkpoint, which slows S-phase progression, stabilizes slowed or stalled replication forks, and relieves inhibition of the ribonucleotide reductase (RNR) complex. To identify novel genes that promote cellular viability after replication stress, the S. cerevisiae non-essential haploid gene deletion set (4812 strains) was screened for sensitivity to the RNR inhibitor hydroxyurea (HU). Strains bearing deletions in either CCR4 or CAF1/POP2, which encode components of the cytoplasmic mRNA deadenylase complex, were particularly sensitive to HU. We found that Ccr4 cooperated with the Dun1 branch of the replication checkpoint, such that ccr4Δ dun1Δ strains exhibited irreversible hypersensitivity to HU and persistent activation of Rad53. Moreover, because ccr4Δ and chk1Δ exhibited epistasis in several genetic contexts, we infer that Ccr4 and Chk1 act in the same pathway to overcome replication stress. A counterscreen for suppressors of ccr4Δ HU sensitivity uncovered mutations in CRT1, which encodes the transcriptional repressor of the DNA-damage-induced gene regulon. Whereas Dun1 is known to inhibit Crt1 repressor activity, we found that Ccr4 regulates CRT1 mRNA poly(A) tail length and may subtly influence Crt1 protein abundance. Simultaneous overexpression of RNR2, RNR3 and RNR4 partially rescued the HU hypersensitivity of a ccr4Δ dun1Δ strain, consistent with the notion that the RNR genes are key targets of Crt1. These results implicate the coordinated regulation of Crt1 via Ccr4 and Dun1 as a crucial nodal point in the response to DNA replication stress.

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“…complex [29][30][31][32][33][34][35] . Indeed, disruption of kinesin-14 alone or in combination with Lrs4 deletion, decreased subtelomeric DSB survival to levels similar to those seen in cells deficient in cohibin or Nup84 (Fig.…”

Section: Resultsmentioning

confidence: 99%

Perinuclear tethers license telomeric DSBs for a broad kinesin- and NPC-dependent DNA repair process

et al. 2015

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DNA double-strand breaks (DSBs) are often targeted to nuclear pore complexes (NPCs) for repair. How targeting is achieved and the DNA repair pathways involved in this process remain unclear. Here, we show that the kinesin-14 motor protein complex (Cik1-Kar3) cooperates with chromatin remodellers to mediate interactions between subtelomeric DSBs and the Nup84 nuclear pore complex to ensure cell survival via break-induced replication (BIR), an error-prone DNA repair process. Insertion of a DNA zip code near the subtelomeric DSB site artificially targets it to NPCs hyperactivating this repair mechanism. Kinesin-14 and Nup84 mediate BIR-dependent repair at non-telomeric DSBs whereas perinuclear telomere tethers are only required for telomeric BIR. Furthermore, kinesin-14 plays a critical role in telomerase-independent telomere maintenance. Thus, we uncover roles for kinesin and NPCs in DNA repair by BIR and reveal that perinuclear telomere anchors license subtelomeric DSBs for this error-prone DNA repair mechanism.

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Kar3 interaction with Cik1 alters motor structure and function

Cited by 35 publications

References 34 publications

Kinesin-14 Family Proteins HSET/XCTK2 Control Spindle Length by Cross-Linking and Sliding Microtubules

Kinesin-14 Family Proteins HSET/XCTK2 Control Spindle Length by Cross-Linking and Sliding Microtubules

Ccr4 contributes to tolerance of replication stress through control ofCRT1mRNA poly(A) tail length

Perinuclear tethers license telomeric DSBs for a broad kinesin- and NPC-dependent DNA repair process

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