sad1

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0005515 protein binding	IPI PMID:14655046 Two-hybrid search for proteins that interact with Sad1 and K...	REMOVE	Summary: Protein binding with Sif1 (Sad1-interacting factor 1), identified in a two-hybrid screen for Sad1 and Kms1 interactors. Reason: Generic protein binding is uninformative. The Sif1 interaction comes from a two-hybrid screen; Sif1 genetically interacts with sad1+ and is needed for septation at high temperature, but no specific molecular function of Sad1 is established by this interaction. Removal does not dispute the reported interaction. Supporting Evidence: PMID:14655046 One of these was named sif1+ (for Sad1-interacting factor) and is required for proper septum formation at high temperature
GO:0005515 protein binding	IPI PMID:14655046 Two-hybrid search for proteins that interact with Sad1 and K...	REMOVE	Summary: Protein binding with the t-SNARE Ufe1, from a two-hybrid screen for Sad1 and Kms1 interactors. Reason: Generic protein binding is uninformative, and the two-hybrid interaction with the ER/nuclear-envelope t-SNARE Ufe1 does not define a Sad1 molecular function. Removal does not dispute the reported interaction. Supporting Evidence: PMID:14655046 Two of them, putative homologues of budding yeast UFE1 (which encodes a t-SNARE)
GO:0005515 protein binding	IPI PMID:14655046 Two-hybrid search for proteins that interact with Sad1 and K...	MODIFY	Summary: Protein binding with the KASH protein Kms1; Sad1 and Kms1 are constitutive membrane-bound SPB components that interact with each other. Reason: The partner is the outer-nuclear-membrane KASH protein Kms1, and the Sad1-Kms1 interaction is the SUN-KASH bridge of the fission-yeast LINC complex. As in the human SUN1/SUN2 reviews, the informative function is GO:0140444 cytoskeleton-nuclear membrane anchor activity (GO has no KASH-binding MF term). Proposed replacements: cytoskeleton-nuclear membrane anchor activity Supporting Evidence: PMID:14655046 Kms1 and Sad1, which are constitutive membrane-bound components of the SPB that interact with each other PMID:30462301 Sad1 is a SUN-domain-containing inner-nuclear-membrane protein, and interacts with a KASH-domain-containing outer-nuclear-membrane Kms1 to form a trans-nuclear-membrane complex which is referred to as a linker of nucleoskeleton and cytoskeleton complex (LINC)
GO:0005515 protein binding	IPI PMID:16111942 Hrs1p/Mcp6p on the meiotic SPB organizes astral microtubule ...	MODIFY	Summary: Protein binding with Kms1, reported in a study of the meiotic SPB protein Hrs1/Mcp6 (abstract-only in cache). Reason: The abstract centres on Hrs1/Mcp6 and does not describe the Sad1-Kms1 assay, but the curator read the full text and the Sad1-Kms1 SUN-KASH interaction is independently well established. The informative function is the SUN-KASH anchor, GO:0140444, consistent with the other Sad1-Kms1 row and with the human SUN reviews. Proposed replacements: cytoskeleton-nuclear membrane anchor activity Supporting Evidence: PMID:24943839 Coupling of the DSB to MTs through the Sad1-Kms1 LINC complex can then promote repair of the DSB by GC using alternate templates
GO:0005515 protein binding	IPI PMID:16615890 Meiotic proteins bqt1 and bqt2 tether telomeres to form the ...	MODIFY	Summary: Protein binding with the meiotic telomere bouquet protein Bqt1 (SPAC6G9.13c); Bqt1-Bqt2 bridge the telomere protein Rap1 to Sad1. Reason: Generic protein binding is uninformative. Sad1 is the inner-nuclear-membrane anchor to which the Bqt1-Bqt2-Rap1 telomere complex is tethered, which is captured by GO:0043495 protein-membrane adaptor activity (already carried by Sad1 via IBA). Proposed replacements: protein-membrane adaptor activity Supporting Evidence: PMID:16615890 together the two proteins form a bridge between Rap1 (a telomere protein) and Sad1 (an SPB protein)
GO:0005515 protein binding	IPI PMID:16615890 Meiotic proteins bqt1 and bqt2 tether telomeres to form the ...	MODIFY	Summary: Protein binding with Bqt1 (same interaction as the SPAC6G9.13c row, recorded against the UniProt accession). Reason: Duplicate of the Bqt1 row. The informative activity is Sad1 acting as the membrane anchor for the telomere-Bqt complex (GO:0043495). Proposed replacements: protein-membrane adaptor activity Supporting Evidence: PMID:16615890 a complex including Bqt1 and Bqt2 is essential for connecting telomeres to the SPB
GO:0005515 protein binding	IPI PMID:23166349 Csi1 links centromeres to the nuclear envelope for centromer...	MODIFY	Summary: Protein binding with Csi1 (SPBC2G2.14), shown by two-hybrid and co-immunoprecipitation; Csi1 links centromeres to Sad1. Reason: Generic protein binding is uninformative. Csi1 bridges kinetochores to Sad1 at the inner nuclear membrane beneath the SPB, and Csi1 localization depends on Sad1. Sad1 therefore acts as the membrane anchor for the centromere-Csi1 complex, captured by GO:0043495 protein-membrane adaptor activity. Proposed replacements: protein-membrane adaptor activity Supporting Evidence: PMID:23166349 Yeast two-hybrid and coimmunoprecipitation analysis demonstrated that full-length Csi1 interacted with Sad1 PMID:23166349 the SUN domain protein Sad1, which is an inner nuclear envelope protein, and Csi1, a nuclear protein that interacts with both Sad1 and components of the kinetochore during interphase
GO:0005515 protein binding	IPI PMID:30462301 Structural insights into chromosome attachment to the nuclea...	REMOVE	Summary: Protein binding with Bqt4: a 14-residue Sad1 peptide (residues 88-101) binds the Bqt4 N-terminal domain in vitro (ITC and crystal structure). Reason: Generic protein binding is uninformative, and the authors state that whether Sad1 binds Bqt4 in vivo, and its functional significance, remain to be determined. No specific function can be assigned from this in vitro peptide interaction. Removal does not dispute the reported interaction. Supporting Evidence: PMID:30462301 Determining whether Sad1 interacts with Bqt4 in vivo and revealing the functional significance of this interaction merit further study.
GO:0005635 nuclear envelope	HDA PMID:16823372 ORFeome cloning and global analysis of protein localization ...	ACCEPT	Summary: Nuclear envelope, from the genome-wide YFP localization study. Reason: Sad1 is an integral inner-nuclear-membrane protein concentrated beneath the SPB; nuclear envelope localization is correct. Supporting Evidence: PMID:28619713 Although the SUN domain–containing protein Sad1 localizes to the inner nuclear membrane (INM) region beneath the SPB constitutively
GO:0005635 nuclear envelope	IBA GO_REF:0000033	ACCEPT	Summary: Nuclear envelope (IBA, SUN family node PTN000308195). Reason: The SUN domain family is a conserved nuclear envelope protein family; Sad1 is the founding fungal member and is an inner nuclear membrane protein. Sad1 appears among the node's experimental sources, as expected. Supporting Evidence: PMID:30462301 Sad1 is a SUN-domain-containing inner-nuclear-membrane protein
GO:0005635 nuclear envelope	IEA GO_REF:0000117	ACCEPT	Summary: Nuclear envelope (ARBA electronic). Reason: Correct, consistent with experimental localization. Supporting Evidence: file:SCHPO/sad1/sad1-uniprot.txt Nucleus membrane; Single-pass membrane
GO:0005637 nuclear inner membrane	IDA PMID:39833200 Centromere positioning orchestrates telomere bouquet formati...	ACCEPT	Summary: Nuclear inner membrane. Reason: Sad1 is a single-pass inner-nuclear-membrane SUN protein with its SUN domain in the perinuclear space; this is its site of action for all its tethering functions. Supporting Evidence: PMID:28619713 we first performed SPA-SIM on cells containing Sad1-mCherry as the fiducial marker, because it is located at the INM
GO:0005816 spindle pole body	IEA GO_REF:0000044	ACCEPT	Summary: Spindle pole body (UniProt subcellular location mapping). Reason: Sad1 is a constitutive SPB-associated protein throughout mitosis and meiosis. Supporting Evidence: PMID:7744953 exclusively associated with the spindle pole body (SPB) throughout the mitotic
GO:0030674 protein-macromolecule adaptor activity	IMP PMID:23166349 Csi1 links centromeres to the nuclear envelope for centromer...	ACCEPT	Summary: Protein-macromolecule adaptor activity: Sad1 is required (with Csi1) to link centromeres to the nuclear envelope. Reason: Sad1 with Csi1 forms the molecular link that attaches centromeres to the inner nuclear membrane near the SPB; the sad1 ts mutant releases Csi1 from the SPB region. The adaptor claim is correct; the more specific child GO:0043495 protein-membrane adaptor activity (Sad1 anchoring the Csi1-kinetochore complex to the membrane) is also held via IBA, so this parent is retained as accurate. Supporting Evidence: PMID:23166349 These data suggest that Sad1 and Csi1 are part of the molecular link between the nuclear envelope and the centromeres PMID:23166349 In this temperature-sensitive sad1 mutant, Csi1-GFP was localized in a diffuse nuclear pattern at restrictive temperature, suggesting that Csi1 depends on Sad1 for localization
GO:0031021 interphase microtubule organizing center	IDA PMID:24943839 A role for nuclear envelope-bridging complexes in homology-d...	KEEP AS NON CORE	Summary: Interphase microtubule organizing center: Sad1-Kms1 foci outside the SPB associate with microtubules and with the gamma-tubulin subunit Alp4. Reason: Non-SPB Sad1-Kms1 foci that associate with microtubules and gamma-tubulin were observed, particularly after DNA damage; a real but minor, context-dependent location compared with the SPB. Supporting Evidence: PMID:24943839 Further, both Sad1 and Kms1 at iMTOCs are found in association with MTs
GO:0031965 nuclear membrane	IEA GO_REF:0000044	ACCEPT	Summary: Nuclear membrane (UniProt subcellular location mapping). Reason: Correct; Sad1 is an integral nuclear membrane protein (inner membrane). Supporting Evidence: file:SCHPO/sad1/sad1-uniprot.txt Nucleus membrane; Single-pass membrane
GO:0032121 meiotic attachment of telomeric heterochromatin to spindle pole body	IPI PMID:16615890 Meiotic proteins bqt1 and bqt2 tether telomeres to form the ...	ACCEPT	Summary: Meiotic attachment of telomeric heterochromatin to spindle pole body, based on the Rap1-Bqt1-Bqt2-Sad1 bridge. Reason: Sad1 is the inner-nuclear-membrane end of the bridge that attaches telomeres (via Rap1 and Bqt1/Bqt2) to the SPB in meiotic prophase. This is a core meiotic function of the Sad1-Kms1 LINC complex. Supporting Evidence: PMID:16615890 together the two proteins form a bridge between Rap1 (a telomere protein) and Sad1 (an SPB protein)
GO:0034993 meiotic nuclear membrane microtubule tethering complex	IBA GO_REF:0000033	ACCEPT	Summary: Meiotic nuclear membrane microtubule tethering complex (IBA). Reason: Sad1 forms the meiotic LINC complex with Kms1 that connects telomeres to the SPB and cytoplasmic microtubules during horsetail movement. The more specific GO:1990612 Sad1-Kms1 LINC complex is an is_a child of this term. Supporting Evidence: PMID:27889481 The linkage between the telomere bouquet and the SPB (on the outer surface of the NE during meiotic prophase) occurs via the LINC complex, which comprises the KASH-domain outer NE protein Kms1 and the SUN-domain inner NE protein Sad1.
GO:0034993 meiotic nuclear membrane microtubule tethering complex	IPI PMID:14655046 Two-hybrid search for proteins that interact with Sad1 and K...	MODIFY	Summary: Meiotic nuclear membrane microtubule tethering complex, based on two-hybrid interaction of Sad1 with Kms2. Reason: The evidence partner is Kms2, the essential KASH protein that pairs with Sad1 at the mitotic SPB (for SPB insertion and centromere coupling), not in a meiosis-specific complex. As in the human SUN1/SUN2 reviews, somatic/mitotic SUN-KASH evidence is better captured by the parent GO:0106094 nuclear membrane microtubule tethering complex. Sad1's meiotic complex membership is retained through the IBA row and GO:1990612. Proposed replacements: nuclear membrane microtubule tethering complex Supporting Evidence: PMID:18692466 This includes an integral outer nuclear membrane protein of the KASH family (Kms2) and two integral inner nuclear membrane proteins, the SUN-domain protein Sad1 and the previously uncharacterized protein Ima1
GO:0035861 site of double-strand break	IDA PMID:24943839 A role for nuclear envelope-bridging complexes in homology-d...	KEEP AS NON CORE	Summary: Site of double-strand break: induced DSBs (Rad52 foci) associate and comigrate with Sad1 in S/G2. Reason: A subset of persistent DSBs associates with Sad1 at the nuclear envelope in an ATR- and resection-dependent manner. Sad1 is an INM protein contacting the damaged chromatin rather than a repair factor loaded onto the lesion; a context-specific location. Supporting Evidence: PMID:24943839 In live cells, we observed a subset of induced DSBs closely associated with Sad1
GO:0035974 meiotic spindle pole body	IDA PMID:16615890 Meiotic proteins bqt1 and bqt2 tether telomeres to form the ...	ACCEPT	Summary: Meiotic spindle pole body. Reason: Sad1 localizes to the SPB throughout meiosis, and the telomere bouquet is tethered to Sad1 at the meiotic SPB. Supporting Evidence: PMID:7744953 exclusively associated with the spindle pole body (SPB) throughout the mitotic
GO:0035974 meiotic spindle pole body	IDA PMID:22438582 Spindle pole body components are reorganized during fission ...	ACCEPT	Summary: Meiotic spindle pole body: Sad1 is constantly observed at SPBs during meiotic prophase. Reason: Direct localization evidence during meiosis. Supporting Evidence: PMID:22438582 Type III also included Sad1, whose budding yeast orthologue (Mps3) is known to localize in close proximity to Cdc31 and Sfi1
GO:0035974 meiotic spindle pole body	IDA PMID:7744953 The product of the spindle formation gene sad1+ associates w...	ACCEPT	Summary: Meiotic spindle pole body (original Sad1 characterization). Reason: Sad1 is associated with the SPB throughout meiosis and changes from a dot to a crescent at meiosis II. Supporting Evidence: PMID:7744953 exclusively associated with the spindle pole body (SPB) throughout the mitotic
GO:0043495 protein-membrane adaptor activity	IBA GO_REF:0000033	ACCEPT	Summary: Protein-membrane adaptor activity (IBA, SUN family node PTN000308195). Reason: SUN proteins anchor partner complexes (KASH proteins across the lumen; telomere, centromere and SPB components on the nucleoplasmic side) to the inner nuclear membrane. For Sad1 this is supported by its anchoring of the Bqt1/Bqt2-Rap1 telomere complex and the Csi1-kinetochore link, and by the SPB-nuclear membrane anchor activity (GO:0106166, a child of this term). Supporting Evidence: PMID:16615890 a complex including Bqt1 and Bqt2 is essential for connecting telomeres to the SPB PMID:23166349 we have identified two factors of a molecular link that attaches and clusters centromeres at the inner nuclear envelope near the SPB
GO:0044732 mitotic spindle pole body	HDA PMID:16823372 ORFeome cloning and global analysis of protein localization ...	ACCEPT	Summary: Mitotic spindle pole body (genome-wide YFP localization). Reason: Consistent with extensive low-throughput evidence. Supporting Evidence: PMID:7744953 exclusively associated with the spindle pole body (SPB) throughout the mitotic
GO:0044732 mitotic spindle pole body	IDA PMID:34133218 Redistribution of centrosomal proteins by centromeres and Po...	ACCEPT	Summary: Mitotic spindle pole body: Sad1 redistributes into a ring at the INM around the SPB at mitotic entry. Reason: Direct super-resolution localization. Supporting Evidence: PMID:34133218 On mitotic entry, Sad1 is redistributed into a ring structure at the INM, mediated in part by centromere interactions.
GO:0044732 mitotic spindle pole body	IDA PMID:7744953 The product of the spindle formation gene sad1+ associates w...	ACCEPT	Summary: Mitotic spindle pole body (original Sad1 characterization). Reason: Sad1 is associated with the SPB throughout the mitotic cycle, independently of microtubules. Supporting Evidence: PMID:7744953 exclusively associated with the spindle pole body (SPB) throughout the mitotic
GO:0044732 mitotic spindle pole body	IDA PMID:9802907 Dynamics of centromeres during metaphase-anaphase transition...	ACCEPT	Summary: Mitotic spindle pole body (Sad1-GFP used as SPB marker). Reason: Sad1-GFP is bound to the SPB throughout the cell cycle. Supporting Evidence: PMID:9802907 was expressed and found to be bound to the SPB throughout the cell cycle
GO:0045141 meiotic telomere clustering	IMP PMID:39833200 Centromere positioning orchestrates telomere bouquet formati...	ACCEPT	Summary: Meiotic telomere clustering, from sad1-2 csi1-delta mutant analysis of telomere positioning. Reason: Sad1 is the inner-nuclear-membrane anchor of the telomere bouquet: Bqt1/Bqt2 bridge Rap1 to Sad1, and the Sad1-Kms1 LINC complex couples telomeres to the SPB and dynein-driven horsetail movement. This IMP adds centromere-telomere crosstalk evidence. Core meiotic function. Supporting Evidence: PMID:39833200 brings telomeres closer to the SPB through the interaction of Bqt1/Bqt2 complex with Sad1, which is enriched beneath the SPB PMID:16615890 a complex including Bqt1 and Bqt2 is essential for connecting telomeres to the SPB
GO:0061497 inner plaque of mitotic spindle pole body	IDA PMID:28619713 Molecular model of fission yeast centrosome assembly determi...	ACCEPT	Summary: Inner plaque of mitotic spindle pole body: SIM places Sad1 as the most nuclear SPB component, at the INM beneath the SPB. Reason: Super-resolution positioning places Sad1 on the nuclear side of the SPB, the region corresponding to the inner (nuclear) plaque. Supporting Evidence: PMID:28619713 Orientation of images along the pole axis was based on Sad1-mCherry relative positioning and the assumption that it is the most nuclear SPB component throughout interphase
GO:0071957 old mitotic spindle pole body	IDA PMID:28619713 Molecular model of fission yeast centrosome assembly determi...	ACCEPT	Summary: Old mitotic spindle pole body. Reason: Sad1 is present at both mother (old) and new SPBs; accurate but not functionally distinguishing. Supporting Evidence: PMID:28619713 whereas Sad1-GFP appears at both poles in early G1
GO:0071958 new mitotic spindle pole body	IDA PMID:28619713 Molecular model of fission yeast centrosome assembly determi...	ACCEPT	Summary: New mitotic spindle pole body. Reason: Sad1 spreads to the bridge and satellite early and is at both poles; accurate. Supporting Evidence: PMID:28619713 whereas Sad1-GFP appears at both poles in early G1
GO:0072766 centromere clustering at the mitotic interphase nuclear envelope	EXP PMID:27889481 Mitotic Nuclear Envelope Breakdown and Spindle Nucleation Ar...	ACCEPT	Summary: Centromere clustering at the mitotic interphase nuclear envelope; the Sad1 N-terminal residues 2-60 confer centromere-LINC association and the sad1.2 allele dissociates centromeres from the SPB. Reason: Direct separation-of-function genetics identifies the Sad1 nucleoplasmic region responsible for centromere-LINC attachment in interphase. Core mitotic function. Supporting Evidence: PMID:27889481 We first generated a series of nested deletions (Figure 2A) in the nucleoplasmic domain of Sad1 and used this series to identify the region, amino acids 2–60, that confers centromere-LINC associations
GO:0072766 centromere clustering at the mitotic interphase nuclear envelope	IMP PMID:23166349 Csi1 links centromeres to the nuclear envelope for centromer...	ACCEPT	Summary: Centromere clustering at the mitotic interphase nuclear envelope (sad1 ts mutant). Reason: Sad1 and Csi1 form the link that attaches and clusters centromeres at the INM near the SPB. Supporting Evidence: PMID:23166349 we have identified two factors of a molecular link that attaches and clusters centromeres at the inner nuclear envelope near the SPB
GO:0090619 meiotic spindle pole	EXP PMID:34346498 Loss of kinesin-8 improves the robustness of the self-assemb...	ACCEPT	Summary: Meiotic spindle pole (cited paper is abstract-only in cache). Reason: The abstract does not mention Sad1, which was presumably used as an SPB/pole marker in the full text; Sad1 is well established at the SPB throughout meiosis, and the meiotic SPB is at the meiotic spindle pole. Deferred to the curator. Supporting Evidence: PMID:7744953 exclusively associated with the spindle pole body (SPB) throughout the mitotic
GO:0106166 spindle pole body-nuclear membrane anchor activity	IMP PMID:28619713 Molecular model of fission yeast centrosome assembly determi...	ACCEPT	Summary: Spindle pole body-nuclear membrane anchor activity. Reason: Sad1 is an INM protein that underlies the SPB constitutively and whose mutation causes SPB insertion/anchoring errors; with its KASH partner Kms2 it holds the SPB at the nuclear envelope. This is the fungal-specific form of SUN anchor function and a core function. Supporting Evidence: PMID:28619713 First, mutation of sad1+ results in SPB insertion errors PMID:28619713 Sad1 could facilitate insertion through a variety of mechanisms, such as activation of Cut12, recruitment of structural proteins that shape, bend, and remodel the membrane and/or recruitment of Kms2.
GO:0140480 mitotic spindle pole body insertion into the nuclear envelope	IMP PMID:28619713 Molecular model of fission yeast centrosome assembly determi...	ACCEPT	Summary: Mitotic spindle pole body insertion into the nuclear envelope. Reason: Sad1 redistributes into rings around the SPB at mitotic entry that precede and correlate with SPB insertion, and sad1 mutants show insertion errors. Supporting Evidence: PMID:28619713 Second, the timing of Sad1 redistribution correlates with that of SPB insertion into the NE PMID:28619713 Our data suggest that Sad1 is present at the SPB early to set up structures that will trigger SPB insertion before the cell even enters mitosis.
GO:0140480 mitotic spindle pole body insertion into the nuclear envelope	IMP PMID:34133218 Redistribution of centrosomal proteins by centromeres and Po...	ACCEPT	Summary: Mitotic spindle pole body insertion into the nuclear envelope (Sad1 ring formation, centromere linkage and Polo). Reason: Centromere-driven Sad1 ring formation is the first step of SPB ring assembly (followed by Kms2, Cut12, Cut11) required for partial NE breakdown and SPB insertion. Supporting Evidence: PMID:34133218 From these data, we propose an order of ring formation that starts with Sad1, followed by Kms2 and Cut12 and then finally Cut11 right before SPB separation. file:SCHPO/sad1/sad1-deep-research-falcon.md The most precise statement is that Sad1 forms an early organizing scaffold for the mitotic membrane-remodeling ring.
GO:1990612 Sad1-Kms1 LINC complex	EXP PMID:24943839 A role for nuclear envelope-bridging complexes in homology-d...	ACCEPT	Summary: Sad1-Kms1 LINC complex: damage-induced Sad1-Kms1 foci couple persistent DSBs to microtubules. Reason: The most specific complex term for Sad1's meiotic/DNA-damage partner. Note that GO:1990612 is defined around DSB repair but is placed is_a GO:0034993 (meiotic tethering complex); the Sad1-Kms1 complex also performs the meiotic telomere-SPB linkage. Supporting Evidence: PMID:24943839 Coupling of the DSB to MTs through the Sad1-Kms1 LINC complex can then promote repair of the DSB by GC using alternate templates
GO:0042393 histone binding	IDA PMID:38773107 The SUN-family protein Sad1 mediates heterochromatin spatial...	NEW	Summary: Histone binding: the Sad1 nucleoplasmic histone-binding motif binds H2A-H2B (not H3-H4); crystal structure and structure-based mutants. Reason: Direct biochemical and structural evidence (GST pull-down, ITC, co-crystal structure, structure-guided sad1-5R mutant) that Sad1 binds H2A-H2B, and that this binding is required for Sad1 distribution throughout the NE and for tethering telomeres and the mating-type locus. This is an activity the Sad1 N-terminus performs itself, not an indirect effect. Non-core relative to the SUN-KASH anchor role. Supporting Evidence: PMID:38773107 Sad1, an inner nuclear membrane SUN-family protein in fission yeast, interacts with histone H2A-H2B but not H3-H4 file:SCHPO/sad1/sad1-deep-research-falcon.md It transforms the view of Sad1 from a largely mechanical SUN scaffold into a direct chromatin-binding organizer with a structurally defined histone interface.

Gene Description

Existing Annotations Review

Core Functions

Spindle pole body anchoring and insertion: Sad1 underlies the SPB at the inner nuclear membrane, anchors it to the nuclear envelope with Kms2, and at mitotic entry forms a ring that initiates local nuclear envelope remodelling and SPB insertion.

Centromere tethering: in interphase the Sad1 nucleoplasmic N-terminus, via Csi1 (and Lem2), anchors kinetochores to the inner nuclear membrane beneath the SPB, maintaining the Rabl configuration and allowing centromere signals to trigger SPB insertion.

References

Suggested Questions for Experts

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Deep Research

Falcon

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