Acetylation of the SUN protein Mps3 by Eco1 regulates its function in nuclear organization

Ghosh, Suman; Gardner, Jennifer M.; Smoyer, Christine J.; Friederichs, Jennifer M.; Unruh, Jay R.; Slaughter, Brian D.; Richard, Alexander; Chisholm, R. D.; Lee, Kenneth K.; Workman, Jerry L.; Jaspersen, Sue L.

doi:10.1091/mbc.e11-07-0600

Cited by 27 publications

(26 citation statements)

References 80 publications

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“…'Erasers' such as Hos1 or Smt4 (SUMO isopeptidase) are not shown. Apart from cohesion-related factors, Eco1 also acetylates Mps that is crucial for duplication of the spindle pole body, telomere motility and the association of the chromosome with the nuclear envelope 3, a nuclear envelope yeast protein (Antoniacci et al, 2007;Antoniacci et al, 2004;Antoniacci and Skibbens, 2006;Ghosh et al, 2012;Haas et al, 2012). these double mutant cells exhibit both conditional lethality and, even at permissive temperatures, extensive cohesion defects that are identical to those observed in cohesin mutant cells (Guacci and Koshland, 2012;Rowland et al, 2009;Sutani et al, 2009;Feytout et al, 2011).…”

Section: Cdc4mentioning

confidence: 99%

Cohesin codes – interpreting chromatin architecture and the many facets of cohesin function

Rudra

Skibbens

2013

Journal of Cell Science

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SummarySister chromatid tethering is maintained by cohesin complexes that minimally contain Smc1, Smc3, Mcd1 and Scc3. During S-phase, chromatin-associated cohesins are modified by the Eco1/Ctf7 family of acetyltransferases. Eco1 proteins function during S phase in the context of replicated sister chromatids to convert chromatin-bound cohesins to a tethering-competent state, but also during G2 and M phases in response to double-stranded breaks to promote error-free DNA repair. Cohesins regulate transcription and are essential for ribosome biogenesis and complete chromosome condensation. Little is known, however, regarding the mechanisms through which cohesin functions are directed. Recent findings reveal that Eco1-mediated acetylation of different lysine residues in Smc3 during S phase promote either cohesion or condensation. Phosphorylation and SUMOylation additionally impact cohesin functions. Here, we posit the existence of a cohesin code, analogous to the histone code introduced over a decade ago, and speculate that there is a symphony of posttranslational modifications that direct cohesins to function across a myriad of cellular processes. We also discuss evidence that outdate the notion that cohesion defects are singularly responsible for cohesion-mutant-cell inviability. We conclude by proposing that cohesion establishment is linked to chromatin formation.

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Section: Cdc4mentioning

confidence: 99%

Cohesin codes – interpreting chromatin architecture and the many facets of cohesin function

Rudra

Skibbens

2013

Journal of Cell Science

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“…Mps3 also directly binds to acetyltransferase Eco1/Ctf7 resulting in post-translational modification of Mps3. Acetylation of Mps3 is required for accurate sister chromatid cohesion and for chromosome recruitment to the nuclear membrane (Antoniacci et al, 2004; Ghosh et al, 2012). Although Csm4, a KASH protein of S. cerevisiae , has been implicated to participate in the Mps3-mediated interphase chromosome tethering (Chan et al, 2011), the role of KASH proteins still remains elusive.…”

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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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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“…For example, in human and C. elegans, SUN1 is phosphorylated in cell cycle progression, and the yeast SUN1 homolog, Mps3, is acetylated in the region upstream of the transmembrane domain during chromosome recruitment to the nuclear membrane. [30][31][32] Third, in addition to variations of oligomer formation and post-translational modification, alternative splicing generates a huge number of SUN and nesprin variants. 4,33,34 The human SUN1 gene is located at chromosome position 7p22.3 and has 22 exons that encode up to 916 amino acids residues.…”

Section: Introductionmentioning

confidence: 99%

SUN1 splice variants, SUN1_888, SUN1_785, and predominant SUN1_916, variably function in directional cell migration

Nishioka

Imaizumi

Imada

et al. 2016

Nucleus

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The LINC complex is a multifunctional protein complex that is involved in various processes at the nuclear envelope, such as nuclear migration, mechanotransduction and chromatin tethering in the meiotic phase. However, it remains unknown how these functions are regulated in different cell contexts. An inner nuclear membrane component of the LINC complex, SUN1, is ubiquitously expressed. The human SUN1 gene produces over 10 variants by alternative splicing. Although functions of SUN1 are relatively well characterized, functional differences among SUN1 splice variants are poorly characterized. LINC complex components are associated with a wide range of human diseases; therefore, it is important to understand the functional diversity among SUN1 splice variants. Here, we identified a novel human SUN1 splice variant, SUN1_888. overexpression of the SUN1 splice variants, SUN1_888 or SUN1_785, but not the predominant isoform, SUN1_916, activated directional cell migration. Knockdown of SUN1_888 suppressed cell migration; in contrast depletion of SUN1_916 activated cell migration. In addition, all of investigated SUN1 splicing variants rescued cell migration in SUN1 knock out cell. These results indicate that redundant and non-redundant functions of SUN1 splice variant in directional cell migration and suggest that variable LINC complexes with distinct task may exit. Furthermore, in contrast to previous studies, we showed association between SUN1 and B-type lamins. Interestingly, B-type lamin preferentially interacts with SUN1 but not SUN2. These results suggest that tissue-specific SUN1 variants variably interact with nucleoplasmic partners and allow variable assembly of LINC complexes that can be assigned to distinct tasks.

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Acetylation of the SUN protein Mps3 by Eco1 regulates its function in nuclear organization

Cited by 27 publications

References 80 publications

Cohesin codes – interpreting chromatin architecture and the many facets of cohesin function

Cohesin codes – interpreting chromatin architecture and the many facets of cohesin function

Making the LINC: SUN and KASH protein interactions

SUN1 splice variants, SUN1_888, SUN1_785, and predominant SUN1_916, variably function in directional cell migration

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