Evidence map›Paper›PMID 35821396›Full record

ArticleScientific reports2022

The conserved C-terminal residues of FAM83H are required for the recruitment of casein kinase 1 to the keratin cytoskeleton.

Takahisa Kuga, Naoki Inoue, Kensuke Sometani, Shino Murataka, Minami Saraya, Rina Sugita, Toshinari Mikami, Yasunori Takeda, Masanari Taniguchi, Kentaro Nishida and 1 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed, 1 pooled it
0.7field-weighted citation impact, top 33% 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

5 citing papers in PubMed, 1 synthesis or guideline pooled it, 8 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Expression ofInternational journal of molecular sciences · 2025
    Article
  4. Article
  5. Casein kinase 1α mediates eryptosis: a review.Apoptosis : an international journal on programmed cell death · 2023
    Review
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

11 authors at 2 institutions in 1 country.

Takahisa KugaLaboratory of Analytics for Biomolecules, Faculty of Pharmaceutical Science, Setsunan University, 45-1 Nagaotoge-cho, Hirakata-shi, Osaka, 573-0101, Japan. takahisa.kuga@pharm.setsunan.ac.jp.
Naoki InoueLaboratory of Analytics for Biomolecules, Faculty of Pharmaceutical Science, Setsunan University, 45-1 Nagaotoge-cho, Hirakata-shi, Osaka, 573-0101, Japan.
Kensuke SometaniLaboratory of Analytics for Biomolecules, Faculty of Pharmaceutical Science, Setsunan University, 45-1 Nagaotoge-cho, Hirakata-shi, Osaka, 573-0101, Japan.
Shino MuratakaLaboratory of Analytics for Biomolecules, Faculty of Pharmaceutical Science, Setsunan University, 45-1 Nagaotoge-cho, Hirakata-shi, Osaka, 573-0101, Japan.
Minami SarayaLaboratory of Analytics for Biomolecules, Faculty of Pharmaceutical Science, Setsunan University, 45-1 Nagaotoge-cho, Hirakata-shi, Osaka, 573-0101, Japan.
Rina SugitaLaboratory of Analytics for Biomolecules, Faculty of Pharmaceutical Science, Setsunan University, 45-1 Nagaotoge-cho, Hirakata-shi, Osaka, 573-0101, Japan.
Toshinari MikamiPax Creation Medical Lab., LLC, Iwate, 020-0805, Japan.
Yasunori TakedaDivision of Clinical Pathology, Department of Reconstructive Oral and Maxillofacial Surgery, School of Dentistry, Iwate Medical University, Iwate, 028-3694, Japan.
Masanari TaniguchiLaboratory of Analytics for Biomolecules, Faculty of Pharmaceutical Science, Setsunan University, 45-1 Nagaotoge-cho, Hirakata-shi, Osaka, 573-0101, Japan.
Kentaro NishidaDepartment of Integrative Pharmaceutical Sciences, Faculty of Pharmaceutical Science, Setsunan University, Osaka, 573-0101, Japan.
Nobuyuki YamagishiLaboratory of Analytics for Biomolecules, Faculty of Pharmaceutical Science, Setsunan University, 45-1 Nagaotoge-cho, Hirakata-shi, Osaka, 573-0101, Japan.
Setsunan University · JPIwate Medical University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The casein kinase 1 (CK1) family of serine/threonine protein kinases is involved in diverse cellular events at discrete subcellular compartments. FAM83H acts as a scaffold protein that recruits CK1 to the keratin cytoskeleton or to the nuclear speckles, which are storage sites for splicing factors. We determined the amino acid region of FAM83H required for recruiting CK1 to the keratin cytoskeleton. The subcellular localization of mutant FAM83H proteins with deletions of amino acid residues at different positions was evaluated via immunofluorescence. FAM83H mutants with deleted C-terminal residues 1134-1139, which are conserved among vertebrates, lost the ability to localize and recruit CK1 to the keratin cytoskeleton, suggesting that these residues are required for recruiting CK1 to the keratin cytoskeleton. The deletion of these residues (1134-1139) translocated FAM83H and CK1 to the nuclear speckles. Amino acid residues 1 to 603 of FAM83H were determined to contain the region responsible for the recruitment of CK1 to the nuclear speckles. Our results indicated that FAM83H recruits CK1 preferentially to the keratin cytoskeleton and alternatively to the nuclear speckles.

Indexed as

Casein Kinase IKeratinsAmino AcidsAnimalsCasein KinasesCytoskeletonMicrotubulesMutant ProteinsAmino AcidsCasein Kinase ICasein KinasesKeratinsMutant Proteins

Identifiers

PMID35821396
PMCPMC9276658
OpenAlexW4285090439

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.