Evidence map›Paper›PMID 19305391›Full record

ArticleEMBO reports2009

RANBP2 is an allosteric activator of the conventional kinesin-1 motor protein, KIF5B, in a minimal cell-free system.

Kyoung-in Cho, Haiqing Yi, Ria Desai, Arthur R Hand, Arthur L Haas, Paulo A Ferreira

Open access · bronzeAbstract read
In one paragraph

Article in EMBO reports, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.7field-weighted citation impact, top 11% 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

36 citing papers in PubMed, 62 citations in OpenAlex.

  1. Review
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  6. The emerging roles of GCN5L1 in mitochondrial and vacuolar organelle biology.Biochimica et biophysica acta. Gene regulatory mechanisms · 2021
    Review
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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 4 institutions in 1 country.

Kyoung-in ChoDepartment of Ophthalmology, Duke University Medical Center, DUEC 3802, Erwin Road, Durham, North Carolina 27710, USA.
Haiqing Yi
Ria Desai
Arthur R Hand
Arthur L Haas
Paulo A Ferreira
Duke Medical Center · USDuke University · USLouisiana State University · USUniversity of Connecticut · US

Funding

VISION RESEARCHP30EY005722 · NEI · DUKE UNIVERSITY · PI Vadim Y Arshavsky · 1985 to 2026
$19.3M
STRUCTURE/FUNCTION ANALYSIS OF RANBP2 IN THE NEURORETINAR01EY011993 · NEI · MEDICAL COLLEGE OF WISCONSIN · PI FERREIRA, PAULO A · 1999 to 2006
$1.8M
NEI NIH HHS 2P30-EY005722-21NEI NIH HHS EY011993NEI NIH HHS P30 EY005722NEI NIH HHS R01 EY011993
6 · The paper itself

Abstract

The association of cargoes to kinesins is thought to promote kinesin activation, yet the validation of such a model with native cargoes is lacking because none is known to activate kinesins directly in an in vitro system of purified components. The RAN-binding protein 2 (RANBP2), through its kinesin-binding domain (KBD), associates in vivo with kinesin-1, KIF5B/KIF5C. Here, we show that KBD and its flanking domains, RAN GTPase-binding domains 2 and 3 (RBD2/RBD3), activate the ATPase activity of KIF5B approximately 30-fold in the presence of microtubules and ATP. The activation kinetics of KIF5B by RANBP2 is biphasic and highly cooperative. Deletion of one of its RBDs lowers the activation of KIF5B threefold and abolishes cooperativity. Remarkably, RBD2-KBD-RBD3 induces unfolding and modest activation of KIF5B in the absence of microtubules. Hence, RANBP2 is the first native and positive allosteric activator known to jump-start and boost directly the activity of a kinesin.

Indexed as

Adenosine TriphosphatasesAllosteric RegulationCell-Free SystemHumansKinesinsKineticsMicrotubulesModels, BiologicalMolecular ChaperonesNuclear Pore Complex ProteinsProtein BindingProtein Structure, TertiaryAdenosine TriphosphatasesKIF5B protein, humanKinesinsMolecular ChaperonesNuclear Pore Complex Proteinsran-binding protein 2

Identifiers

PMID19305391
PMCPMC2680871
OpenAlexW2148905482

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.