Evidence map›Paper›PMID 25326380›Full record

ArticleThe Journal of biological chemistry2014

Arf6 guanine nucleotide exchange factor cytohesin-2 binds to CCDC120 and is transported along neurites to mediate neurite growth.

Tomohiro Torii, Yuki Miyamoto, Kenji Tago, Kazunori Sango, Kazuaki Nakamura, Atsushi Sanbe, Akito Tanoue, Junji Yamauchi

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.2field-weighted citation impact, top 24% 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

7 citing papers in PubMed, 20 citations in OpenAlex.

  1. Physiological and Pathological Roles of the Cytohesin Family in Neurons.International journal of molecular sciences · 2022
    Review
  2. Article
  3. Article
  4. ELMOD1 Stimulates ARF6-GTP Hydrolysis to Stabilize Apical Structures in Developing Vestibular Hair Cells.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2018
    Article
  5. Article
  6. Article
  7. Article
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

8 authors at 4 institutions in 1 country.

Tomohiro ToriiFrom the Department of Pharmacology, National Research Institute for Child Health and Development, Setagaya, Tokyo 157-8535, torii-t@ncchd.go.jp.
Yuki MiyamotoFrom the Department of Pharmacology, National Research Institute for Child Health and Development, Setagaya, Tokyo 157-8535.
Kenji Tagothe Graduate School of Medicine, Jichi Medical University, Shimotsuke, Tochigi 329-0498.
Kazunori Sangothe Amyotrophic Lateral Sclerosis/Neuropathy Project, Tokyo Metropolitan Institute of Medical Science, Setagaya, Tokyo 156-8506.
Kazuaki NakamuraFrom the Department of Pharmacology, National Research Institute for Child Health and Development, Setagaya, Tokyo 157-8535.
Atsushi Sanbethe School of Pharmacy, Iwate Medical University, Morioka, Iwate 020-0023, and.
Akito TanoueFrom the Department of Pharmacology, National Research Institute for Child Health and Development, Setagaya, Tokyo 157-8535.
Junji YamauchiFrom the Department of Pharmacology, National Research Institute for Child Health and Development, Setagaya, Tokyo 157-8535, the Graduate School of Medical and Dental Sciences, Tokyo Medical and Dental University, Bunkyo, Tokyo 113-8510, Japan yamauchi-j@ncchd.go.jp.
National Center For Child Health and Development · JPIwate Medical University · JPJichi Medical University · JPTokyo Metropolitan Institute of Medical Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mechanism of neurite growth is complicated, involving continuous cytoskeletal rearrangement and vesicular trafficking. Cytohesin-2 is a guanine nucleotide exchange factor for Arf6, an Arf family molecular switch protein, controlling cell morphological changes such as neuritogenesis. Here, we show that cytohesin-2 binds to a protein with a previously unknown function, CCDC120, which contains three coiled-coil domains, and is transported along neurites in differentiating N1E-115 cells. Transfection of the small interfering RNA (siRNA) specific for CCDC120 into cells inhibits neurite growth and Arf6 activation. When neurites start to extend, vesicles containing CCDC120 and cytohesin-2 are transported in an anterograde manner rather than a retrograde one. As neurites continue extension, anterograde vesicle transport decreases. CCDC120 knockdown inhibits cytohesin-2 localization into vesicles containing CCDC120 and diffuses cytohesin-2 in cytoplasmic regions, illustrating that CCDC120 determines cytohesin-2 localization in growing neurites. Reintroduction of the wild type CCDC120 construct into cells transfected with CCDC120 siRNA reverses blunted neurite growth and Arf6 activity, whereas the cytohesin-2-binding CC1 region-deficient CCDC120 construct does not. Thus, cytohesin-2 is transported along neurites by vesicles containing CCDC120, and it mediates neurite growth. These results suggest a mechanism by which guanine nucleotide exchange factor for Arf6 is transported to mediate neurite growth.

Indexed as

Amino Acid SequenceBinding SitesCell LineCell NucleusCytoplasmGene Expression RegulationGTPase-Activating ProteinsHumansMolecular Sequence DataNerve Tissue ProteinsNeurogenesisNeuronsProtein BindingProtein Structure, TertiaryProtein TransportRNA, Small InterferingCCDC120 protein, humancytohesin-2GTPase-Activating ProteinsNerve Tissue ProteinsRNA, Small InterferingADP Ribosylation Factor (ARF)GTPaseGuanine Nucleotide Exchange Factor (GEF)Neurite OutgrowthVesicles

Identifiers

PMID25326380
PMCPMC4256328
OpenAlexW2049426759

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.