Evidence map›Paper›PMID 35283190›Full record

ArticleThe Journal of biological chemistry2022

The CLIP-170 N-terminal domain binds directly to both F-actin and microtubules in a mutually exclusive manner.

Yueh-Fu O Wu, Rachel A Miller, Emily O Alberico, Yaobing A P Huang, Annamarie T Bryant, Nora T Nelson, Erin M Jonasson, Holly V Goodson

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

Article in The Journal of biological chemistry, 2022. 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
0.5field-weighted citation impact, top 44% 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, 5 citations in OpenAlex.

  1. Translational cancer research · 2026
    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 1 institution in 1 country.

Yueh-Fu O WuDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA; Integrated Biomedical Sciences Graduate Program, University of Notre Dame, Notre Dame, Indiana, USA.
Rachel A MillerDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA.
Emily O AlbericoDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA.
Yaobing A P HuangDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA; Integrated Biomedical Sciences Graduate Program, University of Notre Dame, Notre Dame, Indiana, USA.
Annamarie T BryantDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA; Integrated Biomedical Sciences Graduate Program, University of Notre Dame, Notre Dame, Indiana, USA.
Nora T NelsonDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA.
Erin M JonassonDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA.
Holly V GoodsonDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA; Integrated Biomedical Sciences Graduate Program, University of Notre Dame, Notre Dame, Indiana, USA; Department of Biological Sciences, University of Notre Dame, Notre Dame, Indiana, USA. Electronic address: hgoodson@nd.edu.
University of Notre Dame · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The cooperation between the actin and microtubule (MT) cytoskeletons is important for cellular processes such as cell migration and muscle cell development. However, a full understanding of how this cooperation occurs has yet to be sufficiently developed. The MT plus-end tracking protein CLIP-170 has been implicated in this actin-MT coordination by associating with the actin-binding signaling protein IQGAP1 and by promoting actin polymerization through binding with formins. Thus far, the interactions of CLIP-170 with actin were assumed to be indirect. Here, we demonstrate using high-speed cosedimentation assays that CLIP-170 can bind to filamentous actin (F-actin) directly. We found that the affinity of this binding is relatively weak but strong enough to be significant in the actin-rich cortex, where actin concentrations can be extremely high. Using CLIP-170 fragments and mutants, we show that the direct CLIP-170-F-actin interaction is independent of the FEED domain, the region that mediates formin-dependent actin polymerization, and that the CLIP-170 F-actin-binding region overlaps with the MT-binding region. Consistent with these observations, in vitro competition assays indicate that CLIP-170-F-actin and CLIP-170-MT interactions are mutually exclusive. Taken together, these observations lead us to speculate that direct CLIP-170-F-actin interactions may function to reduce the stability of MTs in actin-rich regions of the cell, as previously proposed for MT end-binding protein 1.

Indexed as

ActinsMicrotubulesForminsMicrofilament ProteinsMicrotubule-Associated ProteinsNeoplasm ProteinsActinscytoplasmic linker protein 170ForminsMicrofilament ProteinsMicrotubule-Associated ProteinsNeoplasm Proteinsactin–MT crosstalkbundling assaycosedimentation assaysstructural conservation+TIP network

Identifiers

PMID35283190
PMCPMC9062740
OpenAlexW4220732560

What OpenQuestion 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 OpenQuestion graph.