Evidence map›Paper›PMID 30718277›Full record

ArticleThe Journal of biological chemistry2019

PDZK1-interacting protein 1 (PDZK1IP1) traps Smad4 protein and suppresses transforming growth factor-β (TGF-β) signaling.

Souichi Ikeno, Naoko Nakano, Keigo Sano, Takashi Minowa, Wataru Sato, Ryosuke Akatsu, Nobuo Sakata, Nobutaka Hanagata, Makiko Fujii, Fumiko Itoh and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

13 citing papers in PubMed, 29 citations in OpenAlex.

  1. 4-1BBCell reports. Medicine · 2025
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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

11 authors at 4 institutions in 1 country.

Souichi IkenoFrom the Laboratory of Biochemistry, Showa Pharmaceutical University, Machida, Tokyo 194-8543, Japan.
Naoko NakanoFrom the Laboratory of Biochemistry, Showa Pharmaceutical University, Machida, Tokyo 194-8543, Japan.
Keigo SanoFrom the Laboratory of Biochemistry, Showa Pharmaceutical University, Machida, Tokyo 194-8543, Japan.
Takashi MinowaNanotechnology Innovation Station, National Institute of Materials Science, Tsukuba, Ibaraki 305-0047, Japan.
Wataru SatoFrom the Laboratory of Biochemistry, Showa Pharmaceutical University, Machida, Tokyo 194-8543, Japan.
Ryosuke AkatsuFrom the Laboratory of Biochemistry, Showa Pharmaceutical University, Machida, Tokyo 194-8543, Japan.
Nobuo SakataFrom the Laboratory of Biochemistry, Showa Pharmaceutical University, Machida, Tokyo 194-8543, Japan.ORCID 0000-0001-9967-8409
Nobutaka HanagataNanotechnology Innovation Station, National Institute of Materials Science, Tsukuba, Ibaraki 305-0047, Japan.
Makiko FujiiGraduate School of Biomedical and Health Sciences, Hiroshima University, Hiroshima, Hiroshima 734-8553, Japan, and.
Fumiko ItohLaboratory of Cardiovascular Medicine, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo 192-0392, Japan.ORCID 0000-0002-7967-0730
Susumu ItohFrom the Laboratory of Biochemistry, Showa Pharmaceutical University, Machida, Tokyo 194-8543, Japan, sitoh@ac.shoyaku.ac.jp.
Showa Pharmaceutical University · JPNational Institute for Materials Science · JPHiroshima University · JPTokyo University of Pharmacy and Life Sciences · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transforming growth factor (TGF)-β signaling in humans is stringently regulated to prevent excessive TGF-β signaling. In tumors, TGF-β signaling can both negatively and positively regulate tumorigenesis dependent on tumor type, but the reason for these opposite effects is unclear. TGF-β signaling is mainly mediated via the Smad-dependent pathway, and herein we found that PDZK1-interacting protein 1 (PDZK1IP1) interacts with Smad4. PDZK1IP1 inhibited both the TGF-β and the bone morphogenetic protein (BMP) pathways without affecting receptor-regulated Smad (R-Smad) phosphorylation. Rather than targeting R-Smad phosphorylation, PDZK1IP1 could interfere with TGF-β- and BMP-induced R-Smad/Smad4 complex formation. Of note, PDZK1IP1 retained Smad4 in the cytoplasm of TGF-β-stimulated cells. To pinpoint PDZK1IP1's functional domain, we created several PDZK1IP1 variants and found that its middle region, from Phe

Indexed as

Protein Interaction MapsSignal TransductionAnimalsCell Line, TumorCell MovementCell ProliferationHumansMaleMembrane ProteinsMice, Inbred BALB CNeoplasmsPhosphorylationSmad4 ProteinTransforming Growth Factor betaMembrane ProteinsPDZK1IP1 protein, humanPdzk1ip1 protein, mouseSmad4 ProteinTransforming Growth Factor betabone morphogenetic protein (BMP)cell signalingPDZK1-interacting protein 1 (PDZK1IP1)receptor protein serine/threonine kinasesignal transductionSmad4SMAD transcription factortranscriptiontransforming growth factor β (TGF-β)tumor

Identifiers

PMID30718277
PMCPMC6442039
OpenAlexW2913005723

What OpenQuestion holds

Textmetadata
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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.