Evidence map›Paper›PMID 12049630›Full record

ArticleThe Biochemical journal2002

Human tastin, a proline-rich cytoplasmic protein, associates with the microtubular cytoskeleton.

Daita Nadano, Jun Nakayama, Shu-Ichi Matsuzawa, Taka-Aki Sato, Tsukasa Matsuda, Michiko N Fukuda

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

27 citing papers in PubMed, 81 citations in OpenAlex.

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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

6 authors at 2 institutions in 1 country.

Daita NadanoDepartment of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa, Nagoya 464-8601, Japan. nadano@agr.nagoya-u.ac.jp
Jun Nakayama
Shu-Ichi Matsuzawa
Taka-Aki Sato
Tsukasa Matsuda
Michiko N Fukuda
Nagoya University · JPShinshu University · JP

Funding

EXPRESSION AND IN VIVO ROLE OF TROPHININ IN MICER01HD034108 · NICHD · BURNHAM INSTITUTE FOR MEDICAL RESEARCH · PI FUKUDA, MICHIKO N · 1997 to 2002
$686k
MECHANISMS OF FAS-MEDIATED SIGNAL TRANSDUCTIONR01GM055147 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI SATO, TAKA-AKI · 1996 to 2000
$204k
NICHD NIH HHS R01 HD34108NIGMS NIH HHS R01 GM55147
6 · The paper itself

Abstract

Tastin was originally identified as an accessory protein for trophinin, a cell adhesion molecule that potentially mediates the initial attachment of the human embryo to the uterine epithelium. However, no information regarding tastin's function is available to date. The present study is aimed at understanding the role of tastin in mammalian cells. Hence, we examined the intracellular localization of tastin in human cell lines transfected with an expression vector encoding influenza virus haemagglutinin (HA)-tagged tastin. Ectopically expressed HA-tastin was seen as a pattern resembling the fibres that overlap the microtubular cytoskeleton. When HA-tastin-expressing cells were cultured with nocodazole to disrupt microtubule (MT) polymerization, tastin was dispersed to the entire cytoplasm and an MT sedimentation assay showed tastin in the supernatant; however, tastin was sedimented with polymeric MTs in cell lysates not treated with nocodazole. Sedimentation assays using HA-tastin mutants deleted at the N- or C-terminus revealed MT-binding activity associated with the N-terminal basic region of tastin. A yeast two-hybrid screen for tastin-interacting proteins identified Tctex-1, one of the light chains of cytoplasmic dynein, as a tastin-binding protein. Immunoprecipitation and Western-blot analysis confirmed binding of HA-tagged tastin and FLAG (Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys epitope)-tagged Tctex-1 in human cells. Furthermore, in vitro assays have demonstrated the binding between a fusion protein, glutathione S-transferase-Tctex-1, and in vitro translated (35)S-labelled tastin. As Tctex-1 is a component of a MT-based molecular motor, these results suggest that tastin plays an important role in mammalian cells by associating with the microtubular cytoskeleton.

Indexed as

Binding SitesCell Adhesion MoleculesCytoskeletonDNA, ComplementaryGenetic VectorsGlutathione TransferaseHumansImmunohistochemistryMicrotubulesOligopeptidesPeptidesProtein BiosynthesisRecombinant Fusion ProteinsRecombinant ProteinsTranscription, GeneticCell Adhesion MoleculesDNA, ComplementaryFLAG peptideGlutathione TransferaseOligopeptidesPeptidesRecombinant Fusion ProteinsRecombinant ProteinsTROAP protein, human

Identifiers

PMID12049630
PMCPMC1222615
OpenAlexW2034824822

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.