scholarly journals Mps2 links Csm4 and Mps3 to form a telomere-associated LINC complex in budding yeast

2020 ◽  
Vol 3 (12) ◽  
pp. e202000824
Author(s):  
Jinbo Fan ◽  
Hui Jin ◽  
Bailey A Koch ◽  
Hong-Guo Yu
Keyword(s):  
Nuclear Membrane ◽  
Meiotic Recombination ◽  
Budding Yeast ◽  
Transmembrane Proteins ◽  
Yeast Cells ◽  
The Sun ◽  
Linc Complex ◽  
Domain Protein ◽  
Yeast Meiosis ◽  
Sun Domain

The linker of the nucleoskeleton and cytoskeleton (LINC) complex is composed of two transmembrane proteins: the KASH domain protein localized to the outer nuclear membrane and the SUN domain protein to the inner nuclear membrane. In budding yeast, the sole SUN domain protein, Mps3, is thought to pair with either Csm4 or Mps2, two KASH-like proteins, to form two separate LINC complexes. Here, we show that Mps2 mediates the interaction between Csm4 and Mps3 to form a heterotrimeric telomere-associated LINC (t-LINC) complex in budding yeast meiosis. Mps2 binds to Csm4 and Mps3, and all three are localized to the telomere. Telomeric localization of Csm4 depends on both Mps2 and Mps3; in contrast, Mps2’s localization depends on Mps3 but not Csm4. Mps2-mediated t-LINC complex regulates telomere movement and meiotic recombination. By ectopically expressing CSM4 in vegetative yeast cells, we reconstitute the heterotrimeric t-LINC complex and demonstrate its ability to tether telomeres. Our findings therefore reveal the heterotrimeric composition of the t-LINC complex in budding yeast and have implications for understanding variant LINC complex formation.

scholarly journals Mps2 links Csm4 and Mps3 to form a telomere-associated LINC complex in budding yeast

2020 ◽  
Author(s):  
Jinbo Fan ◽  
Hui Jin ◽  
Bailey A. Koch ◽  
Hong-Guo Yu
Keyword(s):  
Nuclear Membrane ◽  
Meiotic Recombination ◽  
Budding Yeast ◽  
Transmembrane Proteins ◽  
Yeast Cells ◽  
Linc Complex ◽  
Domain Protein ◽  
Yeast Meiosis ◽  
Sun Domain ◽  
Variant Formation

AbstractThe linker of the nucleoskeleton and cytoskeleton (LINC) protein complex is composed of a pair of transmembrane proteins: the KASH-domain protein localized to the outer nuclear membrane and the SUN-domain protein to the inner nuclear membrane. In budding yeast, the sole SUN-domain protein, Mps3, is thought to pair with either Csm4 or Mps2, two KASH-like proteins, to form two separate LINC complexes. Here we show that Mps2 mediates the interaction between Csm4 and Mps3 to form a heterotrimeric telomere-associated LINC (t-LINC) in budding yeast meiosis. Mps2 binds to Csm4 and Mps3, and all three are localized to the telomere. Telomeric localization of Csm4 depends on both Mps2 and Mps3; in contrast, Mps2’s localization depends on Mps3 but not Csm4. Mps2-mediated t-LINC regulates telomere movement and meiotic recombination. By ectopically expressing CSM4 in vegetative yeast cells, we reconstitute the heterotrimeric t-LINC and demonstrate its ability to tether telomeres. Our findings therefore reveal the heterotrimeric composition of t-LINC in budding yeast and have implications for understanding LINC variant formation.

scholarly journals Cleavage of the SUN-domain protein Mps3 at its N-terminus regulates centrosome disjunction in budding yeast meiosis

PLoS Genetics ◽  
2017 ◽  
Vol 13 (6) ◽  
pp. e1006830 ◽  
Author(s):  
Ping Li ◽  
Hui Jin ◽  
Bailey A. Koch ◽  
Rebecca L. Abblett ◽  
Xuemei Han ◽  
...  
Keyword(s):  
Budding Yeast ◽  
The Sun ◽  
N Terminus ◽  
Domain Protein ◽  
Yeast Meiosis ◽  
Sun Domain

scholarly journals Role of KASH domain lengths in the regulation of LINC complexes

2019 ◽  
Vol 30 (16) ◽  
pp. 2076-2086 ◽  
Author(s):  
Zeinab Jahed ◽  
Hongyan Hao ◽  
Vyom Thakkar ◽  
Uyen T. Vu ◽  
Venecia A. Valdez ◽  
...  
Keyword(s):  
The Sun ◽  
Linc Complex ◽  
Cellular Functions ◽  
C Elegans ◽  
Physical Forces ◽  
Domain Protein ◽  
Dynamics Simulations ◽  
Sun Domain

The linker of the nucleoskeleton and cytoskeleton (LINC) complex is formed by the conserved interactions between Sad-1 and UNC-84 (SUN) and Klarsicht, ANC-1, SYNE homology (KASH) domain proteins, providing a physical coupling between the nucleoskeleton and cytoskeleton that mediates the transfer of physical forces across the nuclear envelope. The LINC complex can perform distinct cellular functions by pairing various KASH domain proteins with the same SUN domain protein. For example, in Caenorhabditis elegans, SUN protein UNC-84 binds to two KASH proteins UNC-83 and ANC-1 to mediate nuclear migration and anchorage, respectively. In addition to distinct cytoplasmic domains, the luminal KASH domain also varies among KASH domain proteins of distinct functions. In this study, we combined in vivo C. elegans genetics and in silico molecular dynamics simulations to understand the relation between the length and amino acid composition of the luminal KASH domain, and the function of the SUN–KASH complex. We show that longer KASH domains can withstand and transfer higher forces and interact with the membrane through a conserved membrane proximal EEDY domain that is unique to longer KASH domains. In agreement with our models, our in vivo results show that swapping the KASH domains of ANC-1 and UNC-83, or shortening the KASH domain of ANC-1, both result in a nuclear anchorage defect in C. elegans.

scholarly journals Telomeres and centromeres have interchangeable roles in promoting meiotic spindle formation

2015 ◽  
Vol 208 (4) ◽  
pp. 415-428 ◽  
Author(s):  
Alex Fennell ◽  
Alfonso Fernández-Álvarez ◽  
Kazunori Tomita ◽  
Julia Promisel Cooper
Keyword(s):  
Fission Yeast ◽  
Nuclear Membrane ◽  
Meiotic Prophase ◽  
Meiotic Spindle ◽  
The Sun ◽  
Spindle Formation ◽  
Domain Protein ◽  
Bipolar Spindles ◽  
Sun Domain ◽  
Meiosis I

Telomeres and centromeres have traditionally been considered to perform distinct roles. During meiotic prophase, in a conserved chromosomal configuration called the bouquet, telomeres gather to the nuclear membrane (NM), often near centrosomes. We found previously that upon disruption of the fission yeast bouquet, centrosomes failed to insert into the NM at meiosis I and nucleate bipolar spindles. Hence, the trans-NM association of telomeres with centrosomes during prophase is crucial for efficient spindle formation. Nonetheless, in approximately half of bouquet-deficient meiocytes, spindles form properly. Here, we show that bouquet-deficient cells can successfully undergo meiosis using centromere–centrosome contact instead of telomere–centrosome contact to generate spindle formation. Accordingly, forced association between centromeres and centrosomes fully rescued the spindle defects incurred by bouquet disruption. Telomeres and centromeres both stimulate focal accumulation of the SUN domain protein Sad1 beneath the centrosome, suggesting a molecular underpinning for their shared spindle-generating ability. Our observations demonstrate an unanticipated level of interchangeability between the two most prominent chromosomal landmarks.

scholarly journals Involvement of Sir2/4 in Silencing of DNA Breakage and Recombination on Mouse YACs during Yeast Meiosis

2005 ◽  
Vol 16 (3) ◽  
pp. 1449-1455 ◽  
Author(s):  
Yair Klieger ◽  
Ofer Yizhar ◽  
Drora Zenvirth ◽  
Neta Shtepel-Milman ◽  
Margriet Snoek ◽  
...  
Keyword(s):  
Meiotic Recombination ◽  
Hot Spot ◽  
Yeast Cells ◽  
Class Iii ◽  
Dna Double Strand Breaks ◽  
Artificial Chromosomes ◽  
Mouse Major Histocompatibility Complex ◽  
Dna Backbone ◽  
Yeast Meiosis ◽  
Yeast Artificial Chromosomes

Yeast artificial chromosomes (YACs) that contain human DNA backbone undergo DNA double-strand breaks (DSBs) and recombination during yeast meiosis at rates similar to the yeast native chromosomes. Surprisingly, YACs containing DNA covering a recombination hot spot in the mouse major histocompatibility complex class III region do not show meiotic DSBs and undergo meiotic recombination at reduced levels. Moreover, segregation of these YACs during meiosis is seriously compromised. In meiotic yeast cells carrying the mutations sir2 or sir4, but not sir3, these YACs show DSBs, suggesting that a unique chromatin structure of the YACs, involving Sir2 and Sir4, protects the YACs from the meiotic recombination machinery. We speculate that the paucity of DSBs and recombination events on these YACs during yeast meiosis may reflect the refractory nature of the corresponding region in the mouse genome.

scholarly journals Comparative Analysis of Sequence-Structure Function Relationship of the SUN-Domain Protein CaSUN1

2017 ◽  
Vol 05 (03) ◽  
Author(s):  
Poonam Mishra ◽  
Vijay Wardhan ◽  
Aarti Pandey ◽  
Subhra Chakraborty ◽  
Gunjan Garg ◽  
...  
Keyword(s):  
Comparative Analysis ◽  
Structure Function ◽  
The Sun ◽  
Sequence Structure ◽  
Structure Function Relationship ◽  
Domain Protein ◽  
Function Relationship ◽  
Relationship Of ◽  
Sun Domain

scholarly journals Phosphorylation of luminal region of the SUN-domain protein Mps3 promotes nuclear envelope localization during meiosis

2020 ◽  
Author(s):  
H. B. D. Prasada Rao ◽  
Takeshi Sato ◽  
Kiran Challa ◽  
Miki Shinohara ◽  
Akira Shinohara
Keyword(s):  
Protein Kinase ◽  
Nuclear Envelope ◽  
Control Force ◽  
Linc Complex ◽  
Specific Localization ◽  
Domain Protein ◽  
Protein Ensembles ◽  
And Function ◽  
Sun Domain ◽  
Luminal Region

SummaryDuring meiosis, protein ensembles in the nuclear envelope (NE) containing SUN- and KASH-domain proteins, called linker nucleocytoskeleton and cytoskeleton (LINC) complex, promote chromosome motion. How LINC complexes acquire the meiotic property is largely unknown. Here we showed that cyclin-dependent protein kinase (CDK) and Dbf4-dependent Cdc7 protein kinase (DDK) promote proper meiosis-specific localization of yeast SUN-domain protein Mps3 on NE and control force-dependent movement of chromosomes during meiosis. We also found a NE luminal region of Mps3 juxtaposed to inner nuclear membrane (INM) is required for meiosis-specific localization of Mps3 on NE. Negative charges introduced by meiosis-specific non-canonical phosphorylation of the luminal region of Mps3 changes its interaction with INM, which may induce NE localization by promoting the formation of a canonical LINC complex with Mps3. Our study reveals unique phosphorylation-dependent regulation on the localization and function of Mps3 protein in meiotic NE remodeling.

scholarly journals Absence of SUN-domain protein Slp1 blocks karyogamy and switches meiotic recombination and synapsis from homologs to sister chromatids

2014 ◽  
Vol 111 (38) ◽  
pp. E4015-E4023 ◽  
Author(s):  
C. Vasnier ◽  
A. de Muyt ◽  
L. Zhang ◽  
S. Tesse ◽  
N. E. Kleckner ◽  
...  
Keyword(s):  
Meiotic Recombination ◽  
Sister Chromatids ◽  
Domain Protein ◽  
Sun Domain

scholarly journals Making the LINC: SUN and KASH protein interactions

2015 ◽  
Vol 396 (4) ◽  
pp. 295-310 ◽  
Author(s):  
Dae In Kim ◽  
Birendra KC ◽  
Kyle J. Roux
Keyword(s):  
Protein Interactions ◽  
Nuclear Membrane ◽  
Comprehensive Analysis ◽  
Linc Complex ◽  
Protein Protein Interactions ◽  
Cell Nuclei ◽  
Cellular Functions ◽  
The Core ◽  
Sun Domain ◽  
Critical Structure

Abstract Cell nuclei are physically integrated with the cytoskeleton through the linker of nucleoskeleton and cytoskeleton (LINC) complex, 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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