Evidence map›Paper›PMID 27858498›Full record

ArticleNucleus (Austin, Tex.)2016

SUN1 splice variants, SUN1_888, SUN1_785, and predominant SUN1_916, variably function in directional cell migration.

Yu Nishioka, Hiromasa Imaizumi, Junko Imada, Jun Katahira, Nariaki Matsuura, Miki Hieda

Open access · goldAbstract read
In one paragraph

Article in Nucleus (Austin, Tex.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.6field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

34 citing papers in PubMed, 46 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Yu Nishiokaa Osaka University, Graduate School of Medicine and Health Science , Suita City , Osaka , Japan.
Hiromasa Imaizumia Osaka University, Graduate School of Medicine and Health Science , Suita City , Osaka , Japan.
Junko Imadaa Osaka University, Graduate School of Medicine and Health Science , Suita City , Osaka , Japan.
Jun Katahirab Osaka University, Graduate School of Frontier Bioscience , Suita City , Osaka , Japan.
Nariaki Matsuuraa Osaka University, Graduate School of Medicine and Health Science , Suita City , Osaka , Japan.
Miki Hiedaa Osaka University, Graduate School of Medicine and Health Science , Suita City , Osaka , Japan.
Osaka University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The LINC complex is a multifunctional protein complex that is involved in various processes at the nuclear envelope, such as nuclear migration, mechanotransduction and chromatin tethering in the meiotic phase. However, it remains unknown how these functions are regulated in different cell contexts. An inner nuclear membrane component of the LINC complex, SUN1, is ubiquitously expressed. The human SUN1 gene produces over 10 variants by alternative splicing. Although functions of SUN1 are relatively well characterized, functional differences among SUN1 splice variants are poorly characterized. LINC complex components are associated with a wide range of human diseases; therefore, it is important to understand the functional diversity among SUN1 splice variants. Here, we identified a novel human SUN1 splice variant, SUN1_888. overexpression of the SUN1 splice variants, SUN1_888 or SUN1_785, but not the predominant isoform, SUN1_916, activated directional cell migration. Knockdown of SUN1_888 suppressed cell migration; in contrast depletion of SUN1_916 activated cell migration. In addition, all of investigated SUN1 splicing variants rescued cell migration in SUN1 knock out cell. These results indicate that redundant and non-redundant functions of SUN1 splice variant in directional cell migration and suggest that variable LINC complexes with distinct task may exit. Furthermore, in contrast to previous studies, we showed association between SUN1 and B-type lamins. Interestingly, B-type lamin preferentially interacts with SUN1 but not SUN2. These results suggest that tissue-specific SUN1 variants variably interact with nucleoplasmic partners and allow variable assembly of LINC complexes that can be assigned to distinct tasks.

Indexed as

Cell MovementCell LineCell NucleusCytoskeletonGene Expression RegulationHumansLamin Type BMembrane ProteinsMicrotubule-Associated ProteinsNuclear ProteinsProtein IsoformsLamin Type BMembrane ProteinsMicrotubule-Associated ProteinsNuclear ProteinsProtein IsoformsSUN1 protein, humanB-type lamincell migrationlamin B1lamin B2LINC complexsplice variantSUN1SUN2

Identifiers

PMID27858498
PMCPMC5214592
OpenAlexW2553969595

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.