Evidence map›Paper›PMID 15684027›Full record

ArticleThe Journal of cell biology2005

Myosin V attachment to cargo requires the tight association of two functional subdomains.

Natasha Pashkova, Natalie L Catlett, Jennifer L Novak, Guanming Wu, Renne Lu, Robert E Cohen, Lois S Weisman

Abstract read
In one paragraph

Article in The Journal of cell biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
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

18 citing papers in PubMed.

  1. Article
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  9. Article
  10. Review
  11. Article
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  14. Acto-Myosin motorises the flow of auxin.Plant signaling & behavior · 2007
    Article
  15. Review
  16. Article
  17. Article
  18. 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

7 authors.

Natasha PashkovaDepartment of Biochemistry, University of Iowa, Iowa City, IA 52242, USA.
Natalie L Catlett
Jennifer L Novak
Guanming Wu
Renne Lu
Robert E Cohen
Lois S Weisman

Funding

Regulation of myosin V interaction with cargo-Equipment SupplementR01GM062261 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Lois S Weisman · 2001 to 2026
$5.8M
Regulation of Myosin V Interaction with CargoR37GM062261 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI WEISMAN, LOIS S · 2009 to 2018
$4.3M
INTERDISCIPLINARY RESEARCH TRAINING PROGRAM ON AGINGT32AG000214 · NIA · UNIVERSITY OF IOWA · PI WALLACE, ROBERT BRUCE · 1991 to 2000
$164k
NIA NIH HHS T32 AG000214NIA NIH HHS T32 AG 00214NIGMS NIH HHS GM62261NIGMS NIH HHS R01 GM062261NIGMS NIH HHS R37 GM062261
6 · The paper itself

Abstract

The myosin V carboxyl-terminal globular tail domain is essential for the attachment of myosin V to all known cargoes. Previously, the globular tail was viewed as a single, functional entity. Here, we show that the globular tail of the yeast myosin Va homologue, Myo2p, contains two structural subdomains that have distinct functions, namely, vacuole-specific and secretory vesicle-specific movement. Biochemical and genetic analyses demonstrate that subdomain I tightly associates with subdomain II, and that the interaction does not require additional proteins. Importantly, although neither subdomain alone is functional, simultaneous expression of the separate subdomains produces a functional complex in vivo. Our results suggest a model whereby intramolecular interactions between the globular tail subdomains help to coordinate the transport of multiple distinct cargoes by myosin V.

Indexed as

Amino Acid SequenceBinding SitesBiological TransportCytoplasmic VesiclesEscherichia coliGene ExpressionMicrotubule-Associated ProteinsModels, BiologicalMolecular Sequence DataMutationMyosin Heavy ChainsMyosin Type VNuclear ProteinsPeptide FragmentsProtein BindingReceptors, Cell SurfaceKAR9 protein, S cerevisiaekinesin-like protein 1Microtubule-Associated ProteinsMYO2 protein, S cerevisiaeMyosin Heavy ChainsMyosin Type VNuclear ProteinsPeptide FragmentsReceptors, Cell SurfaceRecombinant ProteinsSaccharomyces cerevisiae ProteinsTrypsinVAC17 protein, S cerevisiaeVesicular Transport Proteins

Identifiers

PMID15684027
PMCPMC2171732

What OpenQuestion holds

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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.