Evidence map›Paper›PMID 34154701›Full record

ArticleBMB reports2021

Kinesin-1-dependent transport of the βPIX/GIT complex in neuronal cells.

Eun-Young Shin, Chan-Soo Lee, Han-Byeol Kim, Jin-Hee Park, Kwangseok Oh, Gun-Wu Lee, Eun-Yul Cho, Hyong Kyu Kim, Eung-Gook Kim

Open access · goldAbstract read
PubMed Full text at PMC
In one paragraph

Article in BMB reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.1field-weighted citation impact, top 59% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. 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

9 authors at 2 institutions in 1 country.

Eun-Young ShinDepartments of Biochemistry, College of Medicine, and Medical Research Center, Chungbuk National University, Cheongju 28644, Korea.
Chan-Soo LeeFood Standard Division Scientific Office, Ministry of Food and Drug Safety (KFDA), Cheongju 28159, Korea.
Han-Byeol KimDepartments of Biochemistry, College of Medicine, and Medical Research Center, Chungbuk National University, Cheongju 28644, Korea.
Jin-Hee ParkDepartments of Biochemistry, College of Medicine, and Medical Research Center, Chungbuk National University, Cheongju 28644, Korea.
Kwangseok OhDepartments of Biochemistry, College of Medicine, and Medical Research Center, Chungbuk National University, Cheongju 28644, Korea.
Gun-Wu LeeDepartments of Biochemistry, College of Medicine, and Medical Research Center, Chungbuk National University, Cheongju 28644, Korea.
Eun-Yul ChoDepartments of Biochemistry, College of Medicine, and Medical Research Center, Chungbuk National University, Cheongju 28644, Korea.
Hyong Kyu KimMicrobiology, College of Medicine, and Medical Research Center, Chungbuk National University, Cheongju 28644, Korea.
Eung-Gook KimDepartments of Biochemistry, College of Medicine, and Medical Research Center, Chungbuk National University, Cheongju 28644, Korea.
Chungbuk National University · KRMinistry of Food and Drug Safety · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proper targeting of the βPAK-interacting exchange factor (βPIX)/G protein-coupled receptor kinase-interacting target protein (GIT) complex into distinct cellular compartments is essential for its diverse functions including neurite extension and synaptogenesis. However, the mechanism for translocation of this complex is still unknown. In the present study, we reported that the conventional kinesin, called kinesin-1, can transport the βPIX/GIT complex. Additionally, βPIX bind to KIF5A, a neuronal isoform of kinesin-1 heavy chain, but not KIF1 and KIF3. Mapping analysis revealed that the tail of KIF5s and LZ domain of βPIX were the respective binding domains. Silencing KIF5A or the expression of a variety of mutant forms of KIF5A inhibited βPIX targeting the neurite tips in PC12 cells. Furthermore, truncated mutants of βPIX without LZ domain did not interact with KIF5A, and were unable to target the neurite tips in PC12 cells. These results defined kinesin-1 as a motor protein of βPIX, and may provide new insights into βPIX/GIT complex-dependent neuronal pathophysiology. [BMB Reports 2021; 54(7): 380-385].

Indexed as

AnimalsCell Cycle ProteinsKinesinsNeuronsPC12 CellsProtein IsoformsRatsRho Guanine Nucleotide Exchange FactorsCell Cycle ProteinsGit1 protein, ratKif5A protein, ratKIF5B protein, ratKinesinsProtein IsoformsRho Guanine Nucleotide Exchange Factors

Identifiers

PMID34154701
PMCPMC8328822
OpenAlexW3177348892

What OpenQuestion holds

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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.