Evidence map›Paper›PMID 40210674›Full record

ArticleScientific reports2025

The DUF1669 domain of FAM83H is required for its localization to nuclear speckles.

Takahisa Kuga, Minami Saraya, Sora Higuchi, Shun Yoshida, Shino Murataka, Yuri Fujiwara, Yudai Tomita, Sayo Hayama, Yuichiro Kaibori, Nobuyuki Yamagishi

Abstract read
In one paragraph

Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

2 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
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

10 authors.

Takahisa KugaLaboratory of Analytics for Biomolecules, Faculty of Pharmaceutical Science, Setsunan University, 45-1 Nagaotoge-cho, Hirakata-shi, 573-0101, Osaka, Japan. takahisa.kuga@pharm.setsunan.ac.jp.
Minami SarayaLaboratory of Analytics for Biomolecules, Faculty of Pharmaceutical Science, Setsunan University, 45-1 Nagaotoge-cho, Hirakata-shi, 573-0101, Osaka, Japan.
Sora HiguchiLaboratory of Analytics for Biomolecules, Faculty of Pharmaceutical Science, Setsunan University, 45-1 Nagaotoge-cho, Hirakata-shi, 573-0101, Osaka, Japan.
Shun YoshidaLaboratory of Analytics for Biomolecules, Faculty of Pharmaceutical Science, Setsunan University, 45-1 Nagaotoge-cho, Hirakata-shi, 573-0101, Osaka, Japan.
Shino MuratakaLaboratory of Analytics for Biomolecules, Faculty of Pharmaceutical Science, Setsunan University, 45-1 Nagaotoge-cho, Hirakata-shi, 573-0101, Osaka, Japan.
Yuri FujiwaraLaboratory of Analytics for Biomolecules, Faculty of Pharmaceutical Science, Setsunan University, 45-1 Nagaotoge-cho, Hirakata-shi, 573-0101, Osaka, Japan.
Yudai TomitaLaboratory of Analytics for Biomolecules, Faculty of Pharmaceutical Science, Setsunan University, 45-1 Nagaotoge-cho, Hirakata-shi, 573-0101, Osaka, Japan.
Sayo HayamaLaboratory of Analytics for Biomolecules, Faculty of Pharmaceutical Science, Setsunan University, 45-1 Nagaotoge-cho, Hirakata-shi, 573-0101, Osaka, Japan.
Yuichiro KaiboriLaboratory of Analytics for Biomolecules, Faculty of Pharmaceutical Science, Setsunan University, 45-1 Nagaotoge-cho, Hirakata-shi, 573-0101, Osaka, Japan.
Nobuyuki YamagishiLaboratory of Analytics for Biomolecules, Faculty of Pharmaceutical Science, Setsunan University, 45-1 Nagaotoge-cho, Hirakata-shi, 573-0101, Osaka, Japan.

Funding

Japan Society for the Promotion of Science 24K12893, 21K09865
6 · The paper itself

Abstract

Autosomal-dominant hypocalcified amelogenesis imperfecta (ADHCAI) is caused by mutations in the FAM83H gene. Mutated FAM83H genes encode truncated FAM83H proteins with amino acid lengths between amino acids 1-286 and 1-693, in contrast to wild-type FAM83H (1-1179). Deletion of the C-terminus of FAM83H results in its subcellular translocation from the cytoplasmic compartment to the nuclear speckles, where splicing factors accumulate. However, the amino acid region of FAM83H required for nuclear speckle localization has not yet been determined, and whether all FAM83H-truncated proteins associated with ADHCAI localize to nuclear speckles remains unknown. Here, we examined the subcellular localization of FAM83H mutant proteins with truncations or deletions at various amino acid positions. Deletions within residues 1-300, which corresponds to the DUF1669 domain (17-281), attenuated or abolished the nuclear speckle localization of FAM83H. Meanwhile, some ADHCAI-related FAM83H-truncated proteins did not localize to nuclear speckles, despite the presence of the DUF1669 domain. These results suggest that the DUF1669 domain is required, but not sufficient, for nuclear speckle localization of FAM83H, demonstrating that nuclear speckle localization is not a common feature among FAM83H-truncated proteins related to ADHCAI.

Indexed as

Amelogenesis ImperfectaCell NucleusProteinsHumansProtein DomainsProtein TransportFAM83H protein, humanProteinsAmelogenesis imperfectaCasein kinase IFAM83HNuclear speckles

Identifiers

PMID40210674
PMCPMC11986100

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

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.