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Coiled-coil domains of SUN-1 are required for oligomerization and retention of the protein in the nuclear envelope, especially at later stages of female gametogenesis.
POT-1 (Montrer POT1 Protéines) has a role in anchoring telomeres through SUN-1 at the nuclear periphery.
This suggests that SUN-1 phosphorylation is critical to delaying meiosis in response to perturbed synapsis. SUN-1 may be an integral part of a checkpoint system to monitor establishment of the obligate crossover
The dynamics of matefin/SUN-1 aggregates remained unchanged throughout leptonene/zygotene, despite the progression of pairing.
Data show that ZYG-12 is immobile at the outer nuclear membrane and that SUN-1 is sufficient to localize ZYG-12 in cells.
Data suggest that the properties of the nuclear envelope are altered during the time window when homologs are sorted and Matefin/SUN-1 aggregates form, thereby controling the movement, homologous pairing and interhomolog recombination of chromosomes.
SUN1/SUN2 (Montrer SUN2 Protéines) may function redundantly in early HIV-1 infection steps and therefore influence HIV-1 replication and pathogenesis.
wndchrm revealed a consistent negative correlation between SUN1 expression and the size of nucleoli in human breast cancer tissues.
Nuclear envelope associated endosome-mediated transfer depends on the nuclear envelope proteins SUN1 and SUN2 (Montrer SUN2 Protéines), as well as the Sec61 (Montrer SEC61A1 Protéines) translocon complex.
SUN1 plays a role in hnRNP-involved mRNA export.
An important role for SUN1 and SUN2 (Montrer SUN2 Protéines) in muscle disease pathogenesis.
these data support a model whereby mitotic phosphorylation of SUN1 disrupts interactions with nucleoplasmic binding partners, promoting disassembly of the nuclear lamina and, potentially, its chromatin interactions
The Caenorhabditis elegans lamin, LMN-1, is required for nuclear migration and interacts with the nucleoplasmic domain of the SUN protein UNC-84.
Results highlight the interactions at the nuclear envelope where mutations in the EMD (Montrer EMD Protéines) and TMPO (Montrer TMPO Protéines) gene in combination with mutations in SUN1 have an impact on several components of the network.
Farnesylation of progerin enhances its interaction with SUN1 and reduces SUN1 mobility.
Codepletion of SUN1/2 slows cell proliferation and results in an accumulation of morphologically defective and disoriented mitotic spindles.
Results provide evidence that SUN1 and KASH5 are essential factors in the regulation of meiotic resumption and spindle formation.
A cell-type-specific role for Sun1 and Sun2 (Montrer SUN2 Protéines) in nucleokinesis during cerebellar development, is reported.
ablation of the kinase CDK2 alters the nuclear envelope in mouse spermatocytes, and that the proteins SUN1, KASH5 (also known as CCDC155) and lamin C2 show an abnormal cap-like distribution facing the centrosome.
our results clearly indicate that SUN1 and SUN2 (Montrer SUN2 Protéines), at least partially, fulfill redundant meiotic functions
Sun1, a component of LINC complexes, but not A-type lamins, which interact with LINC complexes at the nuclear envelope, participate in cone nuclei positioning.
Sun1 has a role in DNA damage response.
It was shown KASH5 possesses hitherto unknown KASH-related sequences that directly interacted with SUN1 and mediated telomere localization. KASH5 interacted with the microtubule-associated dynein- dynactin (Montrer DCTN1 Protéines) complex.
These findings implicate Sun1 protein accumulation as a common pathogenic event in Lmna (Montrer LMNA Protéines)(-/-), LmnaDelta9 mice, models for Emery-Dreifuss muscular dystrophy and Hutchinson-Gilford progeria disorders.
Syne-2 (Montrer SYNE2 Protéines), SUN1 and SUN2 (Montrer SUN2 Protéines) play critical roles during interkinetic nuclear migration and photoreceptor cell migration in the mouse retina development.
perturbations in lamin A (Montrer LMNA Protéines)-SUN1 and SUN2 (Montrer SUN2 Protéines) protein interactions may underlie the opposing effects of EDMD (Montrer EMD Protéines) and HGPS (Montrer LMNA Protéines) mutations on nuclear and cellular mechanics
This gene is a member of the unc-84 homolog family and encodes a nuclear nuclear envelope protein with an Unc84 (SUN) domain. The protein is involved in nuclear anchorage and migration. Alternatively spliced transcript variants have been described.
SUN domain-containing protein 1
, Sad1 unc-84 domain protein 1
, protein unc-84 homolog A
, sad1/unc-84 protein-like 1
, unc-84 homolog A