scholarly journals The Drosophila KASH domain proteins Msp-300 and Klarsicht and the SUN domain protein Klaroid have no essential function during oogenesis

Fly ◽  
2008 ◽  
Vol 2 (2) ◽  
pp. 82-91 ◽  
Author(s):  
Martin Technau ◽  
Siegfried Roth
Keyword(s):  
The Sun ◽  
Essential Function ◽  
Domain Protein ◽  
Sun Domain

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 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 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 A conserved KASH domain protein associates with telomeres, SUN1, and dynactin during mammalian meiosis

2012 ◽  
Vol 198 (2) ◽  
pp. 165-172 ◽  
Author(s):  
Akihiro Morimoto ◽  
Hiroki Shibuya ◽  
Xiaoqiang Zhu ◽  
Jihye Kim ◽  
Kei-ichiro Ishiguro ◽  
...  
Keyword(s):  
Germ Cell ◽  
Crucial Role ◽  
Meiotic Chromosome ◽  
Specific Protein ◽  
The Sun ◽  
Chromosome Movement ◽  
Pairing Mechanism ◽  
Domain Protein ◽  
Dynactin Complex ◽  
Sun Domain

In yeasts and worms, KASH (Klarsicht/ANC-1/Syne/homology) domain and SUN (Sad-1/UNC-84) domain nuclear envelope (NE) proteins play a crucial role in meiotic chromosome movement and homologue pairing. However, although the vertebrate SUN domain protein SUN1 is involved in these processes, its partner has remained identified. Based on subcellular localization screening in mouse spermatocytes, we identified a novel germ cell–specific protein, KASH5, that localized exclusively at telomeres from the leptotene to diplotene stages in both spermatocytes and oocytes. KASH5 possesses hitherto unknown KASH-related sequences that directly interacted with SUN1 and mediated telomere localization. Thus, KASH5 is a mammalian meiosis-specific KASH domain protein. We show that meiotic chromosome movement depended on microtubules and that KASH5 interacted with the microtubule-associated dynein–dynactin complex. These results suggest that KASH5 connects the telomere-associated SUN1 protein to the cytoplasmic force–generating mechanism involved in meiotic chromosome movement. Our study strongly suggests that the meiotic homologue-pairing mechanism mediated by the SUN–KASH NE bridge is highly conserved among eukaryotes.

scholarly journals SUNny Ways: The Role of the SUN-Domain Protein Mps3 Bridging Yeast Nuclear Organization and Lipid Homeostasis

2020 ◽  
Vol 11 ◽  
Author(s):  
Maria Laura Sosa Ponce ◽  
Sarah Moradi-Fard ◽  
Vanina Zaremberg ◽  
Jennifer A. Cobb
Keyword(s):  
Nuclear Organization ◽  
Lipid Homeostasis ◽  
The Sun ◽  
Domain Protein ◽  
Sun Domain

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 Yeast telomerase and the SUN domain protein Mps3 anchor telomeres and repress subtelomeric recombination

2009 ◽  
Vol 23 (8) ◽  
pp. 928-938 ◽  
Author(s):  
H. Schober ◽  
H. Ferreira ◽  
V. Kalck ◽  
L. R. Gehlen ◽  
S. M. Gasser
Keyword(s):  
The Sun ◽  
Yeast Telomerase ◽  
Domain Protein ◽  
Sun Domain

scholarly journals DrosophilaklaroidEncodes a SUN Domain Protein Required for Klarsicht Localization to the Nuclear Envelope and Nuclear Migration in the Eye

Fly ◽  
2007 ◽  
Vol 1 (2) ◽  
pp. 75-85 ◽  
Author(s):  
Martin P. Kracklauer ◽  
Susan M.L. Banks ◽  
Xuanhua Xie ◽  
Yaning Wu ◽  
Janice A. Fischer
Keyword(s):  
Nuclear Envelope ◽  
Nuclear Migration ◽  
Domain Protein ◽  
Sun Domain
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