Evidence map›Paper›PMID 20519438›Full record

ArticleMolecular biology of the cell2010

Phosphorylation controls autoinhibition of cytoplasmic linker protein-170.

Ho-Sup Lee, Yulia A Komarova, Elena S Nadezhdina, Rana Anjum, John G Peloquin, Joseph M Schober, Oana Danciu, Jeffrey van Haren, Niels Galjart, Steven P Gygi and 2 more

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

25 citing papers in PubMed, 41 citations in OpenAlex.

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  20. Ordered recruitment of dynactin to the microtubule plus-end is required for efficient initiation of retrograde axonal transport.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013
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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

12 authors at 3 institutions in 2 countries.

Ho-Sup LeeDepartment of Cell and Molecular Biology, Northwestern University Medical School, Chicago, IL 60611, USA.
Yulia A Komarova
Elena S Nadezhdina
Rana Anjum
John G Peloquin
Joseph M Schober
Oana Danciu
Jeffrey van Haren
Niels Galjart
Steven P Gygi
Anna Akhmanova
Gary G Borisy
Northwestern University · USErasmus MC · NLHarvard University · US

Funding

MECHANISM AND CONTROL OF MICROTUBULE ASSEMBLYR01GM025062 · NIGMS · UNIVERSITY OF WISCONSIN MADISON · PI BORISY, GARY G · 1985 to 2003
$1.9M
MECHANISM AND CONTROL OF MICROTUBULE ASSEMBLYR37GM025062 · NIGMS · UNIVERSITY OF WISCONSIN MADISON · PI BORISY, GARY G · 1989 to 1998
–
NIGMS NIH HHS GM-25062NIGMS NIH HHS R01 GM025062NIGMS NIH HHS R37 GM025062
6 · The paper itself

Abstract

Cytoplasmic linker protein (CLIP)-170 is a microtubule (MT) plus-end-tracking protein that regulates MT dynamics and links MT plus ends to different intracellular structures. We have shown previously that intramolecular association between the N and C termini results in autoinhibition of CLIP-170, thus altering its binding to MTs and the dynactin subunit p150(Glued) (J. Cell Biol. 2004: 166, 1003-1014). In this study, we demonstrate that conformational changes in CLIP-170 are regulated by phosphorylation that enhances the affinity between the N- and C-terminal domains. By using site-directed mutagenesis and phosphoproteomic analysis, we mapped the phosphorylation sites in the third serine-rich region of CLIP-170. A phosphorylation-deficient mutant of CLIP-170 displays an "open" conformation and a higher binding affinity for growing MT ends and p150(Glued) as compared with nonmutated protein, whereas a phosphomimetic mutant confined to the "folded back" conformation shows decreased MT association and does not interact with p150(Glued). We conclude that phosphorylation regulates CLIP-170 conformational changes resulting in its autoinhibition.

Indexed as

Amino Acid SequenceAnimalsCell LineCyclic AMP-Dependent Protein KinasesDyneinsMiceMicrotubule-Associated ProteinsMicrotubulesModels, BiologicalMolecular Sequence DataMutationNeoplasm ProteinsOkadaic AcidPhosphorylationPhosphoserineProtein FoldingCyclic AMP-Dependent Protein Kinasescytoplasmic linker protein 170DyneinsMicrotubule-Associated ProteinsNeoplasm ProteinsOkadaic AcidPhosphoserineProteome

Identifiers

PMID20519438
PMCPMC2912352
OpenAlexW2160733334

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.