Evidence map›Paper›PMID 37166445›Full record

ArticleFEBS open bio2023

Diacylglycerol kinase ζ interacts with sphingomyelin synthase 1 and sphingomyelin synthase-related protein via different regions.

Masataka Furuta, Chiaki Murakami, Yuki Numagami, Rika Suzuki, Fumio Sakane

Open access · goldAbstract read
In one paragraph

Article in FEBS open bio, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

3 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Article
  3. 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

5 authors at 1 institution in 1 country.

Masataka FurutaDepartment of Chemistry, Graduate School of Science, Chiba University, Japan.
Chiaki MurakamiDepartment of Chemistry, Graduate School of Science, Chiba University, Japan.ORCID 0000-0003-3645-8382
Yuki NumagamiDepartment of Chemistry, Graduate School of Science, Chiba University, Japan.
Rika SuzukiDepartment of Chemistry, Graduate School of Science, Chiba University, Japan.
Fumio SakaneDepartment of Chemistry, Graduate School of Science, Chiba University, Japan.ORCID 0000-0003-0857-0377
Chiba University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We previously reported that diacylglycerol (DG) kinase (DGK) δ interacts with DG-generating sphingomyelin synthase (SMS)-related protein (SMSr), but not SMS1 or SMS2, via their sterile α motif domains (SAMDs). However, it remains unclear whether other DGK isozymes interact with SMSs. Here, we found that DGKζ, which does not contain SAMD, interacts with SMSr and SMS1, but not SMS2. Deletion mutant analyses demonstrated that SAMD in the N-terminal cytosolic region of SMSr binds to the N-terminal half catalytic domain of DGKζ. However, the C-terminal cytosolic region of SMS1 interacts with the catalytic domain of DGKζ. Taken together, these results indicate that DGKζ associates with SMSr and SMS1 in different manners and suggest that they compose new DG signaling pathways.

Indexed as

Diacylglycerol KinaseIsoenzymesTransferases (Other Substituted Phosphate Groups)Diacylglycerol KinaseIsoenzymesphosphatidylcholine-ceramide phosphocholine transferaseTransferases (Other Substituted Phosphate Groups)diacylglycerol kinasesphingomyelin synthasesphingomyelin synthase-related proteinsterile α motif domain

Identifiers

PMID37166445
PMCPMC10315710
OpenAlexW4376133393

What Socratic 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 Socratic graph.