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

scholarly journals Ribosome biogenesis factors bind a nuclear envelope SUN domain protein to cluster yeast telomeres

2011 ◽  
Vol 30 (18) ◽  
pp. 3799-3811 ◽  
Author(s):  
Chihiro Horigome ◽  
Takafumi Okada ◽  
Kyoko Shimazu ◽  
Susan M Gasser ◽  
Keiko Mizuta
Keyword(s):  
Nuclear Envelope ◽  
Ribosome Biogenesis ◽  
Domain Protein ◽  
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.

unc-83encodes a novel component of the nuclear envelope and is essential for proper nuclear migration

Development ◽  
2001 ◽  
Vol 128 (24) ◽  
pp. 5039-5050 ◽  
Author(s):  
Daniel A. Starr ◽  
Greg J. Hermann ◽  
Christian J. Malone ◽  
William Fixsen ◽  
James R. Priess ◽  
...  
Keyword(s):  
Nuclear Envelope ◽  
Essential Role ◽  
Transmembrane Protein ◽  
Nuclear Lamina ◽  
Nuclear Migration ◽  
C Elegans ◽  
Specific Manner ◽  
Sun Domain ◽  
P Cells

Nuclear migration plays an essential role in the growth and development of a wide variety of eukaryotes. Mutations in unc-84, which encodes a conserved component of the nuclear envelope, have been shown to disrupt nuclear migration in two C. elegans tissues. We show that mutations in unc-83 disrupt nuclear migration in a similar manner in migrating P cells, hyp7 precursors and the intestinal primordium, but have no obvious defects in the association of centrosomes with nuclei or the structure of the nuclear lamina of migrating nuclei. We also show that unc-83 encodes a novel transmembrane protein. We identified three unc-83 transcripts that are expressed in a tissue-specific manner. Antibodies against UNC-83 co-localized to the nuclear envelope with lamin and UNC-84. Unlike UNC-84, UNC-83 localized to only specific nuclei, many of which were migratory. UNC-83 failed to localize to the nuclear envelope in unc-84 mutants with lesions in the conserved SUN domain of UNC-84, and UNC-83 interacted with the SUN domain of UNC-84 in vitro, suggesting that these two proteins function together during nuclear migration. We favor a model in which UNC-84 directly recruits UNC-83 to the nuclear envelope where they help transfer force between the cytoskeleton and the nucleus.

scholarly journals Meiosis‐specific cohesin component, Rec8, promotes the localization of Mps3 SUN domain protein on the nuclear envelope

2018 ◽  
Author(s):  
Jagadeeswara Rao Bommi ◽  
Hanumanthu Bala Durga Prasada Rao ◽  
Kiran Challa ◽  
Mika Higashide ◽  
Kaori Shinmyozu ◽  
...  
Keyword(s):  
Nuclear Envelope ◽  
Domain Protein ◽  
Sun Domain

scholarly journals Ribosome biogenesis factors working with a nuclear envelope SUN domain protein

Nucleus ◽  
2012 ◽  
Vol 3 (1) ◽  
pp. 22-28 ◽  
Author(s):  
Chihiro Horigome ◽  
Keiko Mizuta
Keyword(s):  
Nuclear Envelope ◽  
Ribosome Biogenesis ◽  
Domain Protein ◽  
Sun Domain

scholarly journals Csi1 links centromeres to the nuclear envelope for centromere clustering

2012 ◽  
Vol 199 (5) ◽  
pp. 735-744 ◽  
Author(s):  
Haitong Hou ◽  
Zhou Zhou ◽  
Yu Wang ◽  
Jiyong Wang ◽  
Scott P. Kallgren ◽  
...  
Keyword(s):  
Nuclear Envelope ◽  
Nuclear Protein ◽  
Spindle Pole Body ◽  
Spindle Pole ◽  
High Rate ◽  
Chromosome Loss ◽  
Functional Importance ◽  
Pole Body ◽  
Domain Protein ◽  
Sun Domain

In the fission yeast Schizosaccharomyces pombe, the centromeres of each chromosome are clustered together and attached to the nuclear envelope near the site of the spindle pole body during interphase. The mechanism and functional importance of this arrangement of chromosomes are poorly understood. In this paper, we identified a novel nuclear protein, Csi1, that localized to the site of centromere attachment and interacted with both the inner nuclear envelope SUN domain protein Sad1 and centromeres. Both Csi1 and Sad1 mutants exhibited centromere clustering defects in a high percentage of cells. Csi1 mutants also displayed a high rate of chromosome loss during mitosis, significant mitotic delays, and sensitivity to perturbations in microtubule–kinetochore interactions and chromosome numbers. These studies thus define a molecular link between the centromere and nuclear envelope that is responsible for centromere clustering.

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

eLife ◽  
2021 ◽  
Vol 10 ◽  
Author(s):  
Hanumanthu BD Prasada Rao ◽  
Takeshi Sato ◽  
Kiran Challa ◽  
Yurika Fujita ◽  
Miki Shinohara ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Nuclear Envelope ◽  
Meiotic Chromosome ◽  
Linc Complex ◽  
Dependent Protein ◽  
Domain Protein ◽  
Protein Ensembles ◽  
Chromosome Motion ◽  
Sun Domain ◽  
Luminal Region

During meiosis, protein ensembles in the nuclear envelope (NE) containing SUN- and KASH-domain proteins, called linker nucleocytoskeleton and cytoskeleton (LINC) complex, promote the chromosome motion. Yeast SUN-domain protein, Mps3, forms multiple meiosis-specific ensembles on NE, which show dynamic localisation for chromosome motion; however, the mechanism by which these Mps3 ensembles are formed during meiosis remains largely unknown. Here, we showed that the cyclin-dependent protein kinase (CDK) and Dbf4-dependent Cdc7 protein kinase (DDK) regulate meiosis-specific dynamics of Mps3 on NE, particularly by mediating the resolution of Mps3 clusters and telomere clustering. We also found that the luminal region of Mps3 juxtaposed to the inner nuclear membrane is required for meiosis-specific localisation of Mps3 on NE. Negative charges introduced by meiosis-specific phosphorylation in the luminal region of Mps3 alter its interaction with negatively charged lipids by electric repulsion in reconstituted liposomes. Phospho-mimetic substitution in the luminal region suppresses the localisation of Mps3 via the inactivation of CDK or DDK. Our study revealed multi-layered phosphorylation-dependent regulation of the localisation of Mps3 on NE for meiotic chromosome motion and NE remodelling.

scholarly journals LINCking the Nuclear Envelope to Sperm Architecture

Genes ◽  
2021 ◽  
Vol 12 (5) ◽  
pp. 658
Author(s):  
Francesco Manfrevola ◽  
Florian Guillou ◽  
Silvia Fasano ◽  
Riccardo Pierantoni ◽  
Rosanna Chianese
Keyword(s):  
Nuclear Envelope ◽  
Male Fertility ◽  
Nuclear Architecture ◽  
Sperm Cells ◽  
Bridge Structure ◽  
Linc Complex ◽  
Head Formation ◽  
Morphological Maturation ◽  
Integral Proteins ◽  
Sun Domain

Nuclear architecture undergoes an extensive remodeling during spermatogenesis, especially at levels of spermatocytes (SPC) and spermatids (SPT). Interestingly, typical events of spermiogenesis, such as nuclear elongation, acrosome biogenesis, and flagellum formation, need a functional cooperation between proteins of the nuclear envelope and acroplaxome/manchette structures. In addition, nuclear envelope plays a key role in chromosome distribution. In this scenario, special attention has been focused on the LINC (linker of nucleoskeleton and cytoskeleton) complex, a nuclear envelope-bridge structure involved in the connection of the nucleoskeleton to the cytoskeleton, governing mechanotransduction. It includes two integral proteins: KASH- and SUN-domain proteins, on the outer (ONM) and inner (INM) nuclear membrane, respectively. The LINC complex is involved in several functions fundamental to the correct development of sperm cells such as head formation and head to tail connection, and, therefore, it seems to be important in determining male fertility. This review provides a global overview of the main LINC complex components, with a special attention to their subcellular localization in sperm cells, their roles in the regulation of sperm morphological maturation, and, lastly, LINC complex alterations associated to male infertility.

scholarly journals The Sad1-UNC-84 homology domain in Mps3 interacts with Mps2 to connect the spindle pole body with the nuclear envelope

2006 ◽  
Vol 174 (5) ◽  
pp. 665-675 ◽  
Author(s):  
Sue L. Jaspersen ◽  
Adriana E. Martin ◽  
Galina Glazko ◽  
Thomas H. Giddings ◽  
Garry Morgan ◽  
...  
Keyword(s):  
Nuclear Envelope ◽  
Spindle Pole Body ◽  
Spindle Pole ◽  
Integral Membrane Proteins ◽  
Microtubule Nucleation ◽  
The Core ◽  
Pole Body ◽  
C Terminus ◽  
Bridge Structures ◽  
Sun Domain

The spindle pole body (SPB) is the sole site of microtubule nucleation in Saccharomyces cerevisiae; yet, details of its assembly are poorly understood. Integral membrane proteins including Mps2 anchor the soluble core SPB in the nuclear envelope. Adjacent to the core SPB is a membrane-associated SPB substructure known as the half-bridge, where SPB duplication and microtubule nucleation during G1 occurs. We found that the half-bridge component Mps3 is the budding yeast member of the SUN protein family (Sad1-UNC-84 homology) and provide evidence that it interacts with the Mps2 C terminus to tether the half-bridge to the core SPB. Mutants in the Mps3 SUN domain or Mps2 C terminus have SPB duplication and karyogamy defects that are consistent with the aberrant half-bridge structures we observe cytologically. The interaction between the Mps3 SUN domain and Mps2 C terminus is the first biochemical link known to connect the half-bridge with the core SPB. Association with Mps3 also defines a novel function for Mps2 during SPB duplication.

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