Evidence map›Paper›PMID 11689438›Full record

ArticleThe EMBO journal2001

Recruitment of protein kinase D to the trans-Golgi network via the first cysteine-rich domain.

Y Maeda, G V Beznoussenko, J Van Lint, A A Mironov, V Malhotra

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
2.8field-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

73 citing papers in PubMed, 171 citations in OpenAlex.

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13 more citing papers are in PubMed but not listed here.

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.

Y MaedaCell and Developmental Biology Department, Division of Biology, University of California San Diego, La Jolla, CA 92093-0347, USA.
G V Beznoussenko
J Van Lint
A A Mironov
V Malhotra
University of California, San Diego · US

Funding

Telethon E.0982Telethon E.1105
6 · The paper itself

Abstract

Protein kinase D (PKD) is a cytosolic protein, which upon binding to the trans-Golgi network (TGN) regulates the fission of transport carriers specifically destined to the cell surface. We have found that the first cysteine-rich domain (C1a), but not the second cysteine-rich domain (C1b), is sufficient for the binding of PKD to the TGN. Proline 155 in C1a is necessary for the recruitment of intact PKD to the TGN. Whereas C1a is sufficient to target a reporter protein to the TGN, mutation of serines 744/748 to alanines in the activation loop of intact PKD inhibits its localization to the TGN. Moreover, anti-phospho-PKD antibody, which recognizes only the activated form of PKD, recognizes the TGN-bound PKD. Thus, activation of intact PKD is important for binding to the TGN.

Indexed as

Amino Acid SubstitutionAntibodiesCell LineCysteineEnzyme ActivationGenes, ReporterGlutathione TransferaseHeLa CellsHumansMutagenesis, Site-DirectedPhosphorylationProtein BindingProtein Kinase CProtein Structure, TertiaryProtein TransportRecombinant Fusion ProteinsAntibodiesCysteineGlutathione TransferaseProtein Kinase Cprotein kinase DRecombinant Fusion Proteins

Identifiers

PMID11689438
PMCPMC125696
OpenAlexW2064652576

What OpenQuestion holds

Textmetadata
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.