The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
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The requested target is correctly identified. It is Sad1 from Schizosaccharomyces pombe, UniProt Q09825, encoded by sad1 (ORF aliases supplied by UniProt: SPBC12D12.01/SPBC16H5.01c). The 2024 target-specific study explicitly used Q09825, and its description of Sad1 as a single-pass, inner-nuclear-membrane SUN-family protein agrees with the supplied InterPro SUN1–5/SUN-domain and Pfam Sad1_UNC annotations. Papers concerning proteins called Sad1 in Cryptococcus neoformans or other organisms were excluded from the functional conclusions below. (sun2024thesunfamilyprotein pages 1-2, sun2024thesunfamilyprotein pages 2-3)
Sad1 is not an enzyme or transporter. Its primary function is that of an essential membrane-embedded structural scaffold and force-transmission adaptor. At the inner nuclear membrane, it organizes nuclear-envelope-spanning LINC assemblies with outer-membrane KASH proteins, especially Kms1 and Kms2. This architecture connects nuclear chromatin to the spindle pole body (SPB) and cytoplasmic microtubules. Depending on cell-cycle state, Sad1 supports SPB organization and insertion, centromere/SPB coupling, meiotic telomere movement, positioning of persistent DNA breaks, and peripheral heterochromatin organization. (bestul2021redistributionofcentrosomal pages 1-2, king2008anetworkof pages 1-2, swartz2014arolefor pages 2-3)
Sad1 is the founding fungal member of the Sad1/UNC-84 (SUN) protein family. It is an integral inner-nuclear-membrane protein with one transmembrane helix. Current topology places its N-terminal region—including residues 1–169—on the nucleoplasmic side, where it can contact chromatin, while the C-terminal SUN region projects into the nuclear-envelope lumen/perinuclear space and associates with KASH proteins in the outer membrane. This trans-envelope SUN–KASH assembly constitutes a LINC complex. (sun2024thesunfamilyprotein pages 1-2, king2008anetworkof pages 1-2, sun2024thesunfamilyprotein pages 2-3)
Its dominant localization is the nuclear envelope and SPB attachment region. Sad1 defines the membrane region occupied by the SPB and is also detectable at interphase microtubule-organizing centers. Endogenous Sad1–GFP colocalizes with the SPB component Sid4–mCherry. More sensitive imaging found weak additional nuclear-envelope puncta in more than 82% of cells, averaging 2.9 ± 1.2 puncta per cell. These non-SPB puncta depend on an N-terminal histone-binding motif, whereas SPB localization does not. (king2008anetworkof pages 1-2, sun2024thesunfamilyprotein pages 3-4)
The classical genetic literature identifies Sad1 as essential and required for normal SPB function, although the retrieved foundational evidence summarized rather than reproduced the original deletion/conditional-mutant measurements. Accordingly, “essential SPB/inner-nuclear-membrane scaffold” is a strong annotation, but precise lethality penetrance should be taken from the original Hagan and Yanagida study. (king2008anetworkof pages 11-12)
Sad1’s unifying role is to couple otherwise separate structures across the nuclear envelope:
Thus, Sad1 converts nuclear-envelope position into mechanical and organizational control. It should be annotated principally as a SUN-domain LINC-complex component/SPB-associated nuclear-envelope organizer, rather than as a generic signaling protein. Different adaptors retarget the same core scaffold to centromeres in vegetative growth, telomeres during meiosis, and persistent DNA lesions during repair. (king2008anetworkof pages 1-2, swartz2014arolefor pages 2-3, yamamoto2014gatheringupmeiotic pages 2-4)
| Functional module | Precise mechanistic role | Strongest direct evidence / quantitative result | Key source/date |
|---|---|---|---|
| Identity and topology | S. pombe Sad1 (UniProt Q09825) is a conserved, single-pass integral inner-nuclear-membrane SUN protein. Its N-terminal residues 1–169 face the nucleoplasm; the C-terminal SUN region lies in the nuclear-envelope lumen and engages KASH-family partners to form LINC bridges. | Direct: The Q09825-targeted study identifies one transmembrane helix and experimentally uses the nucleoplasmic N terminus for chromatin-binding assays. Independent cell-biological work identifies Sad1 as an integral inner-nuclear-membrane SUN protein interacting with Kms1/Kms2. (sun2024thesunfamilyprotein pages 1-2, king2008anetworkof pages 1-2, sun2024thesunfamilyprotein pages 2-3) | Sun et al., Nature Communications, May 2024; King et al., Cell, 8 Aug 2008 |
| SPB association and mitotic nuclear-envelope remodeling | Sad1 anchors/organizes the spindle-pole-body (SPB) attachment site and redistributes around duplicated SPBs into a ring that precedes localized nuclear-envelope breakdown and SPB insertion. | Direct: Structured-illumination microscopy showed Sad1 ring formation around the SPB; Sad1 is required for recruitment/redistribution of Kms2, Cut12 and Cut11 into the ring. Model: Centromere linkage initiates Sad1 redistribution, while Plo1 activity promotes redistribution of other ring proteins and completion of localized envelope breakdown. (bestul2021redistributionofcentrosomal pages 1-2) | Bestul et al., Molecular Biology of the Cell, online 16 Jun 2021; issue date 1 Aug 2021 |
| Interphase centromere tethering and nuclear mechanics | The Sad1-containing inner-membrane attachment site participates in coupling centromeric heterochromatin to the SPB and cytoplasmic microtubules, maintaining the Rabl configuration and buffering cytoskeletal forces on the nucleus. | Direct: Sad1 defines the microtubule-organizing-centre attachment site and associates with Kms1/Kms2; disruption of the Ima1-mediated heterochromatin connection produces defective coupling, abnormal nuclear shape and loss/mislocalization of SPB and SUN–KASH components. Inference: Sad1 is the membrane scaffold in the Ima1/Csi1-dependent centromere-to-SPB linkage rather than the sole direct centromere receptor. (king2008anetworkof pages 1-2, yadav2018sad1spatiotemporallyregulates pages 2-3) | King et al., Cell, 8 Aug 2008 |
| Meiotic telomere bouquet and horsetail movement | During meiotic prophase, Sad1-containing LINC assemblies connect telomeres to the nuclear envelope/SPB; cytoplasmic microtubules and dynein then move the SPB and attached nucleus, promoting homolog alignment and pairing. | Evidence synthesis: Sad1 relocates from its mitotic SPB pattern to meiotic telomeres; this localization depends on meiosis-specific Bqt1/Bqt2, with Bqt1–Bqt2–Rap1 connecting the telomeric apparatus. Dynein loss severely impairs horsetail movement and homolog pairing. Caution: The force-transmission mechanism is supported at the pathway/LINC level; the excerpted evidence does not quantify a Sad1-specific mutant phenotype. (katsumata2017positionmattersmultiple pages 1-3, yamamoto2014gatheringupmeiotic pages 2-4, yamamoto2014gatheringupmeiotic pages 12-13) | Yamamoto, Cellular and Molecular Life Sciences, Jan 2014; Katsumata et al., Current Genetics, May 2017 |
| Persistent DNA-double-strand-break response | In S/G2, resected persistent breaks can associate with damage-induced Sad1–Kms1 LINC assemblies and cytoplasmic microtubules, increasing break mobility and influencing repair-pathway choice. | Direct: About 25% of induced ade3 breaks and 40% of ade8 breaks comigrated with Sad1 for ≥10 min; some remained associated for >30 min. Approximately 40% of ade8 breaks comigrated with Kms1, and about three-quarters of MMS-induced Sad1 foci lay along microtubules. Recruitment required Rad3/ATR and Exo1-mediated resection, occurred in S/G2 rather than G1, and preferentially induced Kms1 rather than Kms2 foci. Caution: The gathered excerpt does not supply numerical HR-versus-NHEJ outcomes. (swartz2014arolefor pages 2-3, swartz2014arolefor pages 10-11) | Swartz et al., Molecular Biology of the Cell, Aug 2014 |
| H2A–H2B recognition and peripheral heterochromatin | A nucleoplasmic Sad1 histone-binding motif (HBM; residues 110–140) directly recognizes H2A–H2B, enabling Sad1 distribution away from the SPB, tethering telomeres and the mating-type locus to the nuclear envelope, and reinforcing heterochromatin through Clr3/Sir2 recruitment and histone-enhanced condensation. | Direct: A Sad1(110–126)–H2A/H2B structure was solved at 2.15 Å. Sad1(1–169) bound H2A–H2B with Kd 7.5 ± 1.0 μM and H2A.Z–H2B with Kd 7.5 ± 0.9 μM, but not H3–H4. F118 occupies an H2B hydrophobic pocket; the D114R/E117R/F118R/E121R/E122R “5R” mutant abolished binding. Wild-type Sad1 formed weak envelope puncta in >82% of cells (2.9 ± 1.2 puncta/cell); 5R or HBM deletion retained SPB localization but lost this distribution. H2A–H2B improved apparent Clr3 binding from 42.9 to 10.3 μM, whereas Sad1-5R/H2A–H2B remained 47.2 μM. Mutants detached telomeres and the mating-type locus and impaired silencing; histone-enhanced Sad1 droplets recruited Clr3 and Sir2. (sun2024thesunfamilyprotein pages 2-3, sun2024thesunfamilyprotein pages 3-4, sun2024thesunfamilyprotein pages 4-5, sun2024thesunfamilyprotein pages 5-6, sun2024thesunfamilyprotein pages 6-7) | Sun et al., Nature Communications, May 2024 |
Table: Evidence map for the verified Schizosaccharomyces pombe Sad1/Q09825 protein, separating direct experimental findings from mechanistic models or pathway-level inference. Quantitative structural, biochemical, imaging and DNA-repair results are included where available.
During interphase, the bulky cytoplasmic portion of the fission-yeast SPB lies on the cytoplasmic face of the nuclear envelope. At mitotic entry, the SPB must enter a localized nuclear-envelope fenestra so that it can nucleate spindle microtubules inside the nucleus. Super-resolution microscopy showed that Sad1 redistributes around duplicated SPBs into complete or partial rings. Kms2, Cut12, and Cut11 subsequently form related SPB rings; their proper redistribution depends on Sad1 and on centromere–SPB linkage. (bestul2021redistributionofcentrosomal pages 1-2)
The leading mechanistic model is that centromere attachment first drives Sad1 redistribution. Plo1/Polo kinase activity is not required for Sad1’s initial redistribution but is required for effective reorganization of other ring proteins and completion of localized nuclear-envelope breakdown. The resulting membrane remodeling permits SPB insertion and formation of a functional intranuclear spindle. This interpretation is supported by microscopy and perturbation experiments, although the exact molecular action by which a Sad1 ring changes membrane curvature or permeability remains unresolved. (bestul2021redistributionofcentrosomal pages 1-2)
Sad1 therefore participates in SPB duplication/insertion and anchoring, but it should not be described as the catalytic executor of membrane fenestration. Cut11, Brr6, Plo1, centromere attachment, and additional SPB proteins act with it. The most precise statement is that Sad1 forms an early organizing scaffold for the mitotic membrane-remodeling ring. (bestul2021redistributionofcentrosomal pages 1-2, bestul2021redistributionofcentrosomal pages 14-14)
In vegetatively growing fission yeast, centromeres cluster near the SPB, producing the Rabl chromosome arrangement. Sad1 is part of the inner-membrane/SPB attachment platform through which centromeric heterochromatin is coupled to cytoplasmic microtubules. Kms1/Kms2 provide the outer-membrane side; proteins such as Ima1 and Csi1 contribute nuclear chromatin/kinetochore connections. Disrupting the Ima1-mediated connection causes abnormal nuclear shape and loss or displacement of SPB and SUN–KASH components, indicating that the chromatin tether also buffers forces transmitted by cytoplasmic microtubules. (king2008anetworkof pages 1-2, yadav2018sad1spatiotemporallyregulates pages 2-3)
This role is partly direct and partly network-dependent. Sad1 is the indispensable membrane scaffold, but it is not established as the only direct centromere receptor. Indeed, the 2024 histone-binding mutant retained a single clustered Cnp1/CENP-A focus at the SPB, showing that the newly defined H2A–H2B-binding motif is dispensable for centromere clustering. Earlier work assigns a distinct contribution to Sad1’s N-terminal 60 residues. Thus, Sad1 contains separable functional modules for centromere/SPB coupling and broader heterochromatin tethering. (sun2024thesunfamilyprotein pages 9-10, sun2024thesunfamilyprotein pages 4-5)
The most important recent advance is the demonstration that Sad1 directly recognizes histone H2A–H2B. Sun and colleagues published this work in Nature Communications in May 2024 (DOI: 10.1038/s41467-024-48418-7). GST pull-down, size-exclusion chromatography, isothermal titration calorimetry, and endogenous co-immunoprecipitation showed that Sad1 residues 1–169 bind H2A–H2B but not H3–H4. Reported dissociation constants were 7.5 ± 1.0 μM for H2A–H2B and 7.5 ± 0.9 μM for H2A.Z–H2B, indicating little discrimination between canonical H2A and H2A.Z in these assays. (sun2024thesunfamilyprotein pages 2-3, sun2024thesunfamilyprotein pages 1-2)
The minimal histone-binding motif lies at Sad1 residues 110–140. A Sad1 peptide–H2A/H2B complex was solved at 2.15 Å resolution. Sad1 F118 occupies a hydrophobic H2B pocket formed by Y42, I54, and M59, while D114, E117, E121, and E122 provide electrostatic contacts. F118A weakened binding to 76.9 ± 23.1 μM, F118R reduced affinity to poorer than 200 μM, and histone-interface mutations H2A-R79E and H2B-Y42R yielded 90.1 ± 25.5 μM and 44.8 ± 13.7 μM, respectively. Combining D114R/E117R/F118R/E121R/E122R in the sad1-5R allele abolished detectable H2A–H2B binding. (sun2024thesunfamilyprotein pages 3-4, sun2024thesunfamilyprotein pages 4-5)
In cells, sad1-5R and deletion of the histone-binding motif removed Sad1’s dispersed nuclear-envelope localization while preserving its SPB focus. These mutants displaced telomere clusters and the mating-type locus from the nuclear periphery but did not disrupt centromere clustering. Sad1 also colocalized with the heterochromatin protein Swi6 and was enriched at telomeres by ChIP-qPCR. Localization assays scored approximately 85–120 cells per Sad1 genotype, while telomere/mating-type positioning experiments included about 200 cells in individual experiments. (sun2024thesunfamilyprotein pages 3-4, sun2024thesunfamilyprotein pages 4-5, sun2024thesunfamilyprotein pages 5-6)
The same interaction contributes to silencing at subtelomeres, the mating-type locus, and selected pericentromeric repeats. H2A–H2B enhanced Sad1 association with the histone deacetylases Clr3 and Sir2: an apparent Clr3-binding value improved from 42.9 μM for Sad1 alone to 10.3 μM in the Sad1/H2A–H2B condition, whereas Sad1-5R/H2A–H2B remained weak at 47.2 μM. Telomeric Sir2 enrichment decreased and mating-type-locus H3K9 acetylation increased in sad1-5R. (sun2024thesunfamilyprotein pages 6-7)
Sad1 also showed histone-enhanced liquid–liquid phase-separation behavior in vitro. Clr3 and Sir2 did not independently form comparable liquid droplets but partitioned into Sad1-containing condensates; most Clr3–GFP signal near the nuclear envelope recovered within approximately 40 seconds after photobleaching. The authors’ model is that H2A–H2B binding both anchors Sad1 to peripheral heterochromatin and promotes dynamic condensates that concentrate histone deacetylases. This is a compelling model supported by structure-guided mutations and cellular phenotypes, but the physiological necessity of phase separation—as distinct from multivalent binding—will require further separation-of-function experiments. (sun2024thesunfamilyprotein pages 9-10, sun2024thesunfamilyprotein pages 6-7)
A structural caveat is important: the bound Sad1 peptide would clash with DNA in an intact canonical nucleosome. H2A–H2B may therefore bind Sad1 when locally exposed, exchanged, partially unwrapped, or present in a non-nucleosomal pool. The exact physiological histone substrate remains an active mechanistic question. (sun2024thesunfamilyprotein pages 4-5)
At meiotic entry, chromosome organization is reprogrammed: centromeres detach from the SPB and telomeres gather there, forming the bouquet. Sad1 relocates to telomere-associated sites, and this recruitment depends on the meiosis-specific Bqt1/Bqt2 adaptor system. Bqt1–Bqt2 associates with Rap1, which is connected to telomeric Taz1, while Bqt3/Bqt4 contribute telomere–nuclear-envelope attachment. The Sad1–Kms LINC apparatus then couples these chromosome ends to the cytoplasmic microtubule system. (katsumata2017positionmattersmultiple pages 1-3, yamamoto2014gatheringupmeiotic pages 2-4)
Cytoplasmic dynein pulls on SPB-derived microtubules to produce the characteristic back-and-forth “horsetail” movement of the nucleus. Bouquet formation and movement improve homolog alignment, pairing, and recombination while suppressing inappropriate contacts. Dynein-chain depletion severely compromises nuclear movement and homolog pairing, and defects in telomere clustering also impair pairing. These outcomes establish the pathway’s biological importance, although the retrieved evidence does not provide a quantitative phenotype uniquely attributable to a sad1 separation-of-function allele. (yamamoto2014gatheringupmeiotic pages 2-4, yamamoto2014gatheringupmeiotic pages 12-13)
The functional interpretation is therefore that Sad1 is the inner-membrane mechanical coupler in the meiotic telomere–LINC–SPB–microtubule axis; Bqt/Rap1/Taz1 proteins confer telomere specificity, and Kms/dynein/microtubules provide the cytoplasmic force pathway.
Sad1-containing LINC assemblies are also induced at persistent DNA double-strand breaks in S/G2. Rad52-marked breaks could remain associated with oscillating Sad1–GFP/SPB structures for more than 30 minutes. Approximately 25% of induced breaks at ade3 and 40% at ade8 comigrated with Sad1 for at least 10 minutes; about 40% of ade8 breaks also comigrated with Kms1. Roughly three-quarters of MMS-induced Sad1 foci lay along microtubules. (swartz2014arolefor pages 2-3)
Recruitment required Rad3/ATR and Exo1-dependent long-range resection, was not observed for G1-arrested breaks, and preferentially involved Kms1 rather than Kms2. The data support a mechanism in which resected, persistent lesions are connected to cytoplasmic microtubules through Sad1–Kms1, increasing lesion mobility and affecting homology-directed repair-pathway choice. The study directly assayed repair outcomes in at least three experiments with at least 300 cells per condition, but the retrieved text did not expose the exact homologous-recombination versus end-joining percentages; those values are therefore not asserted here. (swartz2014arolefor pages 2-3, swartz2014arolefor pages 10-11)
The 2024 H2A–H2B study is the principal recent Sad1-specific mechanistic advance. It transforms the view of Sad1 from a largely mechanical SUN scaffold into a direct chromatin-binding organizer with a structurally defined histone interface. By comparison, the 2021 Sad1-ring work refined the mechanism of SPB insertion and localized nuclear-envelope breakdown. Together, these studies show that Sad1 integrates membrane mechanics with genome organization. (bestul2021redistributionofcentrosomal pages 1-2, sun2024thesunfamilyprotein pages 2-3)
There is no clinical or industrial implementation of Sad1 itself. Its real-world value is as a research platform:
Molecular function: Essential inner-nuclear-membrane SUN-domain structural adaptor; component of Kms1/Kms2-containing LINC complexes; direct H2A–H2B-binding protein through an N-terminal histone-binding motif; organizer of SPB-associated nuclear-envelope remodeling.
Biological processes: SPB duplication/anchoring and mitotic insertion; localized nuclear-envelope breakdown; centromere–SPB coupling and Rabl chromosome organization; nuclear mechanics; meiotic telomere bouquet formation and horsetail movement; persistent double-strand-break positioning and repair-pathway regulation; telomere and mating-type-locus tethering; peripheral heterochromatin silencing.
Cellular component: Inner nuclear membrane, nuclear envelope, SPB attachment region/SPB-associated ring, meiotic telomere attachment sites, and damage-induced nuclear-envelope foci.
Catalytic activity/substrate: None known. H2A–H2B is a binding partner rather than an enzymatic substrate. Sad1 has no established catalytic reaction or transporter substrate.
The strongest evidence supports Sad1 as a multifunctional structural organizer whose core activity is physical coupling across the nuclear envelope. SPB remodeling, chromosome anchorage, and force transmission are established by genetics and microscopy; H2A–H2B recognition is additionally supported by direct biochemistry and crystallography. Claims that Sad1 itself catalyzes membrane breakdown, recruits every chromosome class directly, or enzymatically modifies chromatin would overstate the evidence. (bestul2021redistributionofcentrosomal pages 1-2, king2008anetworkof pages 1-2, sun2024thesunfamilyprotein pages 2-3)
Key unresolved issues include how Sad1’s SUN domain is structurally coupled to Kms1 versus Kms2, how its binding partners are exchanged between mitosis and meiosis, what physiological form of H2A–H2B engages Sad1 given the predicted clash with nucleosomal DNA, and whether phase separation is required in vivo or merely accompanies multivalent heterochromatin assembly. Quantitative mapping of Sad1 phosphorylation and other cell-cycle modifications also remains an important route to explaining how one membrane scaffold executes these distinct programs.
References
(sun2024thesunfamilyprotein pages 1-2): Wenqi Sun, Qianhua Dong, Xueqing Li, Jinxin Gao, Xianwen Ye, Chunyi Hu, Fei Li, and Yong Chen. The sun-family protein sad1 mediates heterochromatin spatial organization through interaction with histone h2a-h2b. Nature Communications, May 2024. URL: https://doi.org/10.1038/s41467-024-48418-7, doi:10.1038/s41467-024-48418-7. This article has 7 citations and is from a highest quality peer-reviewed journal.
(sun2024thesunfamilyprotein pages 2-3): Wenqi Sun, Qianhua Dong, Xueqing Li, Jinxin Gao, Xianwen Ye, Chunyi Hu, Fei Li, and Yong Chen. The sun-family protein sad1 mediates heterochromatin spatial organization through interaction with histone h2a-h2b. Nature Communications, May 2024. URL: https://doi.org/10.1038/s41467-024-48418-7, doi:10.1038/s41467-024-48418-7. This article has 7 citations and is from a highest quality peer-reviewed journal.
(bestul2021redistributionofcentrosomal pages 1-2): Andrew J. Bestul, Zulin Yu, Jay R. Unruh, and Sue L. Jaspersen. Redistribution of centrosomal proteins by centromeres and polo kinase controls partial nuclear envelope breakdown in fission yeast. Aug 2021. URL: https://doi.org/10.1091/mbc.e21-05-0239, doi:10.1091/mbc.e21-05-0239. This article has 15 citations and is from a domain leading peer-reviewed journal.
(king2008anetworkof pages 1-2): Megan C. King, Theodore G. Drivas, and Günter Blobel. A network of nuclear envelope membrane proteins linking centromeres to microtubules. Cell, 134:427-438, Aug 2008. URL: https://doi.org/10.1016/j.cell.2008.06.022, doi:10.1016/j.cell.2008.06.022. This article has 213 citations and is from a highest quality peer-reviewed journal.
(swartz2014arolefor pages 2-3): Rebecca K. Swartz, Elisa C. Rodriguez, and Megan C. King. A role for nuclear envelope–bridging complexes in homology-directed repair. Molecular Biology of the Cell, 25:2461-2471, Aug 2014. URL: https://doi.org/10.1091/mbc.e13-10-0569, doi:10.1091/mbc.e13-10-0569. This article has 90 citations and is from a domain leading peer-reviewed journal.
(sun2024thesunfamilyprotein pages 3-4): Wenqi Sun, Qianhua Dong, Xueqing Li, Jinxin Gao, Xianwen Ye, Chunyi Hu, Fei Li, and Yong Chen. The sun-family protein sad1 mediates heterochromatin spatial organization through interaction with histone h2a-h2b. Nature Communications, May 2024. URL: https://doi.org/10.1038/s41467-024-48418-7, doi:10.1038/s41467-024-48418-7. This article has 7 citations and is from a highest quality peer-reviewed journal.
(king2008anetworkof pages 11-12): Megan C. King, Theodore G. Drivas, and Günter Blobel. A network of nuclear envelope membrane proteins linking centromeres to microtubules. Cell, 134:427-438, Aug 2008. URL: https://doi.org/10.1016/j.cell.2008.06.022, doi:10.1016/j.cell.2008.06.022. This article has 213 citations and is from a highest quality peer-reviewed journal.
(yamamoto2014gatheringupmeiotic pages 2-4): Ayumu Yamamoto. Gathering up meiotic telomeres: a novel function of the microtubule-organizing center. Cellular and Molecular Life Sciences, 71:2119-2134, Jan 2014. URL: https://doi.org/10.1007/s00018-013-1548-1, doi:10.1007/s00018-013-1548-1. This article has 23 citations and is from a domain leading peer-reviewed journal.
(yadav2018sad1spatiotemporallyregulates pages 2-3): Vikas Yadav and Kaustuv Sanyal. Sad1 spatiotemporally regulates kinetochore clustering to ensure high-fidelity chromosome segregation in the human fungal pathogen cryptococcus neoformans. Aug 2018. URL: https://doi.org/10.1128/msphere.00190-18, doi:10.1128/msphere.00190-18. This article has 25 citations and is from a peer-reviewed journal.
(katsumata2017positionmattersmultiple pages 1-3): Kazuhiro Katsumata, Eriko Nishi, Sadia Afrin, Kaoru Narusawa, and Ayumu Yamamoto. Position matters: multiple functions of linc-dependent chromosome positioning during meiosis. Current Genetics, 63:1037-1052, May 2017. URL: https://doi.org/10.1007/s00294-017-0699-2, doi:10.1007/s00294-017-0699-2. This article has 8 citations and is from a peer-reviewed journal.
(yamamoto2014gatheringupmeiotic pages 12-13): Ayumu Yamamoto. Gathering up meiotic telomeres: a novel function of the microtubule-organizing center. Cellular and Molecular Life Sciences, 71:2119-2134, Jan 2014. URL: https://doi.org/10.1007/s00018-013-1548-1, doi:10.1007/s00018-013-1548-1. This article has 23 citations and is from a domain leading peer-reviewed journal.
(swartz2014arolefor pages 10-11): Rebecca K. Swartz, Elisa C. Rodriguez, and Megan C. King. A role for nuclear envelope–bridging complexes in homology-directed repair. Molecular Biology of the Cell, 25:2461-2471, Aug 2014. URL: https://doi.org/10.1091/mbc.e13-10-0569, doi:10.1091/mbc.e13-10-0569. This article has 90 citations and is from a domain leading peer-reviewed journal.
(sun2024thesunfamilyprotein pages 4-5): Wenqi Sun, Qianhua Dong, Xueqing Li, Jinxin Gao, Xianwen Ye, Chunyi Hu, Fei Li, and Yong Chen. The sun-family protein sad1 mediates heterochromatin spatial organization through interaction with histone h2a-h2b. Nature Communications, May 2024. URL: https://doi.org/10.1038/s41467-024-48418-7, doi:10.1038/s41467-024-48418-7. This article has 7 citations and is from a highest quality peer-reviewed journal.
(sun2024thesunfamilyprotein pages 5-6): Wenqi Sun, Qianhua Dong, Xueqing Li, Jinxin Gao, Xianwen Ye, Chunyi Hu, Fei Li, and Yong Chen. The sun-family protein sad1 mediates heterochromatin spatial organization through interaction with histone h2a-h2b. Nature Communications, May 2024. URL: https://doi.org/10.1038/s41467-024-48418-7, doi:10.1038/s41467-024-48418-7. This article has 7 citations and is from a highest quality peer-reviewed journal.
(sun2024thesunfamilyprotein pages 6-7): Wenqi Sun, Qianhua Dong, Xueqing Li, Jinxin Gao, Xianwen Ye, Chunyi Hu, Fei Li, and Yong Chen. The sun-family protein sad1 mediates heterochromatin spatial organization through interaction with histone h2a-h2b. Nature Communications, May 2024. URL: https://doi.org/10.1038/s41467-024-48418-7, doi:10.1038/s41467-024-48418-7. This article has 7 citations and is from a highest quality peer-reviewed journal.
(bestul2021redistributionofcentrosomal pages 14-14): Andrew J. Bestul, Zulin Yu, Jay R. Unruh, and Sue L. Jaspersen. Redistribution of centrosomal proteins by centromeres and polo kinase controls partial nuclear envelope breakdown in fission yeast. Aug 2021. URL: https://doi.org/10.1091/mbc.e21-05-0239, doi:10.1091/mbc.e21-05-0239. This article has 15 citations and is from a domain leading peer-reviewed journal.
(sun2024thesunfamilyprotein pages 9-10): Wenqi Sun, Qianhua Dong, Xueqing Li, Jinxin Gao, Xianwen Ye, Chunyi Hu, Fei Li, and Yong Chen. The sun-family protein sad1 mediates heterochromatin spatial organization through interaction with histone h2a-h2b. Nature Communications, May 2024. URL: https://doi.org/10.1038/s41467-024-48418-7, doi:10.1038/s41467-024-48418-7. This article has 7 citations and is from a highest quality peer-reviewed journal.
(katsumata2016ataz1and pages 18-19): Kazuhiro Katsumata, Ami Hirayasu, Junpei Miyoshi, Eriko Nishi, Kento Ichikawa, Kazuki Tateho, Airi Wakuda, Hirotada Matsuhara, and Ayumu Yamamoto. A taz1- and microtubule-dependent regulatory relationship between telomere and centromere positions in bouquet formation secures proper meiotic divisions. PLOS Genetics, 12:e1006304, Sep 2016. URL: https://doi.org/10.1371/journal.pgen.1006304, doi:10.1371/journal.pgen.1006304. This article has 10 citations and is from a domain leading peer-reviewed journal.