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Actin dynamics at pointed ends regulates thin filament length in striated muscle

Academic Article
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Overview

related to degree

  • Littlefield, Ryan Scott, Ph.D. in Cell Biology, Scripps Research 1994 - 2000

authors

  • Littlefield, Ryan Scott
  • Almenar-Queralt, A.
  • Fowler, Velia

publication date

  • June 2001

journal

  • Nature Cell Biology  Journal

abstract

  • Regulation of actin dynamics at filament ends determines the organization and turnover of actin cytoskeletal structures. In striated muscle, it is believed that tight capping of the fast-growing (barbed) ends by CapZ and of the slow-growing (pointed) ends by tropomodulin (Tmod) stabilizes the uniform lengths of actin (thin) filaments in myofibrils. Here we demonstrate for the first time that both CapZ and Tmod are dynamic on the basis of the rapid incorporation of microinjected rhodamine-labelled actin (rho-actin) at both barbed and pointed ends and from the photobleaching of green fluorescent protein (GFP)-labelled Tmod. Unexpectedly, the inhibition of actin dynamics at pointed ends by GFP-Tmod overexpression results in shorter thin filaments, whereas the inhibition of actin dynamics at barbed ends by cytochalasin D has no effect on length. These data demonstrate that the actin filaments in myofibrils are relatively dynamic despite the presence of capping proteins, and that regulated actin assembly at pointed ends determines the length of thin filaments.

subject areas

  • Actin Cytoskeleton
  • Actins
  • Acute-Phase Proteins
  • Animals
  • Carrier Proteins
  • Cells, Cultured
  • Chickens
  • Cytochalasin D
  • Green Fluorescent Proteins
  • Luminescent Proteins
  • Microfilament Proteins
  • Muscle, Skeletal
  • Myocardium
  • Tropomodulin
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Identity

International Standard Serial Number (ISSN)

  • 1465-7392

Digital Object Identifier (DOI)

  • 10.1038/35078517

PubMed ID

  • 11389438
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Additional Document Info

start page

  • 544

end page

  • 551

volume

  • 3

issue

  • 6

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