Evidence map›Paper›PMID 20335501›Full record

ArticleMolecular biology of the cell2010

The spectraplakin Short stop is an actin-microtubule cross-linker that contributes to organization of the microtubule network.

Derek A Applewhite, Kyle D Grode, Darby Keller, Alireza Dehghani Zadeh, Alireza Zadeh, Kevin C Slep, Stephen L Rogers

Erratum issuedOpen 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. An erratum has been issued. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

56 citing papers in PubMed, 110 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Septins mediate a microtubule-actin crosstalk that enables actin growth on microtubules.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  7. TheMolecular biology of the cell · 2022
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. New twists in actin-microtubule interactions.Molecular biology of the cell · 2021
    Review
  13. Article
  14. Microtubules: Evolving roles and critical cellular interactions.Experimental biology and medicine (Maywood, N.J.) · 2019
    Review
  15. Microtubules in cell migration.Essays in biochemistry · 2019
    Review
  16. Article
  17. Article
  18. Review
  19. Review
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
    Zadeh, Alireza [corrected to Zadeh, Alireza Dehghani]
5 · Who and what money

Authors and funding

7 authors at 2 institutions in 2 countries.

Derek A ApplewhiteDepartment of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
Kyle D Grode
Darby Keller
Alireza Dehghani Zadeh
Alireza Zadeh
Kevin C Slep
Stephen L Rogers
University of North Carolina at Chapel Hill · USUniversity of British Columbia · CA

Funding

UNC Developmental Biology Training ProgramT32HD046369 · NICHD · UNIV OF NORTH CAROLINA CHAPEL HILL · PI MAGNUSON, TERRY R · 2005 to 2009
$1.4M
Mechanisms of cytoskeletal crosstalk during cellular motilityR01GM081645 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ROGERS, STEPHEN · 2008 to 2012
$1.3M
NICHD NIH HHS T32 HD046369NICHD NIH HHS T32 HD046369-05NIGMS NIH HHS R01 GM-081645NIGMS NIH HHS R01 GM081645
6 · The paper itself

Abstract

The dynamics of actin and microtubules are coordinated in a variety of cellular and morphogenetic processes; however, little is known about the molecules mediating this cytoskeletal cross-talk. We are studying Short stop (Shot), the sole Drosophila spectraplakin, as a model actin-microtubule cross-linking protein. Spectraplakins are an ancient family of giant cytoskeletal proteins that are essential for a diverse set of cellular functions; yet, we know little about the dynamics of spectraplakins and how they bridge actin filaments and microtubules. In this study we describe the intracellular dynamics of Shot and a structure-function analysis of its role as a cytoskeletal cross-linker. We find that Shot interacts with microtubules using two different mechanisms. In the cell interior, Shot binds growing plus ends through an interaction with EB1. In the cell periphery, Shot associates with the microtubule lattice via its GAS2 domain, and this pool of Shot is actively engaged as a cross-linker via its NH(2)-terminal actin-binding calponin homology domains. This cross-linking maintains microtubule organization by resisting forces that produce lateral microtubule movements in the cytoplasm. Our results provide the first description of the dynamics of these important proteins and provide key insight about how they function during cytoskeletal cross-talk.

Indexed as

ActinsAnimalsCytoskeletal ProteinsCytoskeletonDrosophilaMicrotubulesMorphogenesisProtein BindingActinsCytoskeletal Proteins

Identifiers

PMID20335501
PMCPMC2869377
OpenAlexW2074525543

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.