Evidence map›Paper›PMID 17200416›Full record

ArticleThe Journal of cell biology2007

Kinesin-1 structural organization and conformational changes revealed by FRET stoichiometry in live cells.

Dawen Cai, Adam D Hoppe, Joel A Swanson, Kristen J Verhey

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 100 papers.

0numbers the graph read from it
0cells of the map it votes in
100citing papers in PubMed
5.3field-weighted citation impact, top 4% 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

100 citing papers in PubMed, 167 citations in OpenAlex.

  1. Article
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  8. Article
  9. Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025
    Review
  10. Light-Inducible Deformation of Mitochondria in Live Cells.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

40 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Dawen CaiBiophysics Research Division, University of Michigan, Ann Arbor, MI 48109, USA.
Adam D Hoppe
Joel A Swanson
Kristen J Verhey
University of Michigan–Ann Arbor · USHeliophysics · US

Funding

Regulation of the molecular motor kinesin-IR01GM070862 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI VERHEY, KRISTEN J. · 2005 to 2018
$4.2M
Cellular Biotechnology Training Program (CBTP) - Years 31-35T32GM145304 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Guizhi Zhu · 2022 to 2026
$2.6M
MANIPULATION OF PHAGOCYTOSIS IN MACROPHAGESR01AI035950 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SWANSON, JOEL A · 1994 to 2008
$2.2M
Coordination of signaling during phagocytosisR01AI064668 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SWANSON, JOEL A · 2005 to 2010
$1.6M
NIAID NIH HHS AI64668NIAID NIH HHS R01 AI035950NIAID NIH HHS R01 AI064668NIGMS NIH HHS GM070862NIGMS NIH HHS R01 GM070862NIGMS NIH HHS T32 GM145304
6 · The paper itself

Abstract

Kinesin motor proteins drive the transport of cellular cargoes along microtubule tracks. How motor protein activity is controlled in cells is unresolved, but it is likely coupled to changes in protein conformation and cargo association. By applying the quantitative method fluorescence resonance energy transfer (FRET) stoichiometry to fluorescent protein (FP)-labeled kinesin heavy chain (KHC) and kinesin light chain (KLC) subunits in live cells, we studied the overall structural organization and conformation of Kinesin-1 in the active and inactive states. Inactive Kinesin-1 molecules are folded and autoinhibited such that the KHC tail blocks the initial interaction of the KHC motor with the microtubule. In addition, in the inactive state, the KHC motor domains are pushed apart by the KLC subunit. Thus, FRET stoichiometry reveals conformational changes of a protein complex in live cells. For Kinesin-1, activation requires a global conformational change that separates the KHC motor and tail domains and a local conformational change that moves the KHC motor domains closer together.

Indexed as

Fluorescence Resonance Energy TransferAnimalsCell SurvivalChlorocebus aethiopsCOS CellsEnzyme ActivationHumansKinesinsMicrotubule-Associated ProteinsModels, BiologicalProtein Structure, TertiaryProtein SubunitsProtein TransportRatsRecombinant Fusion ProteinsKinesinsMicrotubule-Associated ProteinsProtein SubunitsRecombinant Fusion Proteins

Identifiers

PMID17200416
PMCPMC2063625
OpenAlexW2004240092

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.