schliessen

Filtern

 

Bibliotheken

X-ray diffraction evidence for myosin-troponin connections and tropomyosin movement during stretch activation of insect flight muscle

Stretch activation is important in the mechanical properties of vertebrate cardiac muscle and essential to the flight muscles of most insects. Despite decades of investigation, the underlying molecular mechanism of stretch activation is unknown. We investigated the role of recently observed connecti... Full description

Journal Title: Proceedings of the National Academy of Sciences 04 January 2011, Vol.108(1), p.120
Main Author: Robert J. Perz-Edwards
Other Authors: Thomas C. Irving , Bruce A. J. Baumann , David Gore , Daniel C. Hutchinson , Uroš Kržič , Rebecca L. Porter , Andrew B. Ward , Michael K. Reedy
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 0027-8424 ; E-ISSN: 1091-6490 ; DOI: 10.1073/pnas.1014599107
Zum Text:
SendSend as email Add to Book BagAdd to Book Bag
Staff View
recordid: pnas_s108_1_120
title: X-ray diffraction evidence for myosin-troponin connections and tropomyosin movement during stretch activation of insect flight muscle
format: Article
creator:
  • Robert J. Perz-Edwards
  • Thomas C. Irving
  • Bruce A. J. Baumann
  • David Gore
  • Daniel C. Hutchinson
  • Uroš Kržič
  • Rebecca L. Porter
  • Andrew B. Ward
  • Michael K. Reedy
subjects:
  • Sciences (General)
ispartof: Proceedings of the National Academy of Sciences, 04 January 2011, Vol.108(1), p.120
description: Stretch activation is important in the mechanical properties of vertebrate cardiac muscle and essential to the flight muscles of most insects. Despite decades of investigation, the underlying molecular mechanism of stretch activation is unknown. We investigated the role of recently observed connections between myosin and troponin, called “troponin bridges,” by analyzing real-time X-ray diffraction “movies” from sinusoidally stretch-activated Lethocerus muscles. Observed changes in X-ray reflections arising from myosin heads, actin filaments, troponin, and tropomyosin were consistent with the hypothesis that troponin bridges are the key agent of mechanical signal transduction. The time-resolved sequence of molecular changes suggests a mechanism for stretch activation, in which troponin bridges mechanically tug tropomyosin aside to relieve tropomyosin’s steric blocking of myosin–actin binding. This enables subsequent force production, with cross-bridge targeting further enhanced by stretch-induced lattice compression and thick-filament twisting. Similar linkages may operate in other muscle systems, such as mammalian cardiac muscle, where stretch activation is thought to aid in cardiac ejection.
language: eng
source:
identifier: ISSN: 0027-8424 ; E-ISSN: 1091-6490 ; DOI: 10.1073/pnas.1014599107
fulltext: fulltext_linktorsrc
issn:
  • 0027-8424
  • 00278424
  • 1091-6490
  • 10916490
url: Link


@attributes
ID1336950249
RANK0.07
NO1
SEARCH_ENGINEprimo_central_multiple_fe
SEARCH_ENGINE_TYPEPrimo Central Search Engine
LOCALfalse
PrimoNMBib
record
control
sourcerecordid108_1_120
sourceidpnas_s
recordidTN_pnas_s108_1_120
sourcesystemPC
dbid
0PNE
1RNA
pqid822924192
galeid246534487
display
typearticle
titleX-ray diffraction evidence for myosin-troponin connections and tropomyosin movement during stretch activation of insect flight muscle
creatorRobert J. Perz-Edwards ; Thomas C. Irving ; Bruce A. J. Baumann ; David Gore ; Daniel C. Hutchinson ; Uroš Kržič ; Rebecca L. Porter ; Andrew B. Ward ; Michael K. Reedy
ispartofProceedings of the National Academy of Sciences, 04 January 2011, Vol.108(1), p.120
identifier
subjectSciences (General)
descriptionStretch activation is important in the mechanical properties of vertebrate cardiac muscle and essential to the flight muscles of most insects. Despite decades of investigation, the underlying molecular mechanism of stretch activation is unknown. We investigated the role of recently observed connections between myosin and troponin, called “troponin bridges,” by analyzing real-time X-ray diffraction “movies” from sinusoidally stretch-activated Lethocerus muscles. Observed changes in X-ray reflections arising from myosin heads, actin filaments, troponin, and tropomyosin were consistent with the hypothesis that troponin bridges are the key agent of mechanical signal transduction. The time-resolved sequence of molecular changes suggests a mechanism for stretch activation, in which troponin bridges mechanically tug tropomyosin aside to relieve tropomyosin’s steric blocking of myosin–actin binding. This enables subsequent force production, with cross-bridge targeting further enhanced by stretch-induced lattice compression and thick-filament twisting. Similar linkages may operate in other muscle systems, such as mammalian cardiac muscle, where stretch activation is thought to aid in cardiac ejection.
languageeng
source
version9
lds50peer_reviewed
links
openurl$$Topenurl_article
openurlfulltext$$Topenurlfull_article
linktorsrc$$Uhttp://www.pnas.org/content/108/1/120.abstract$$EView_full_text_in_National_Academy_of_Sciences_(Access_to_full_text_may_be_restricted)
search
creatorcontrib
0Robert J. Perz-Edwards
1Thomas C. Irving
2Bruce A. J. Baumann
3David Gore
4Daniel C. Hutchinson
5Uroš Kržič
6Rebecca L. Porter
7Andrew B. Ward
8Michael K. Reedy
titleX-ray diffraction evidence for myosin-troponin connections and tropomyosin movement during stretch activation of insect flight muscle
description

Stretch activation is important in the mechanical properties of vertebrate cardiac muscle and essential to the flight muscles of most insects. Despite decades of investigation, the underlying molecular mechanism of stretch activation is unknown. We investigated the role of recently observed connections between myosin and troponin, called “troponin bridges,” by analyzing real-time X-ray diffraction “movies” from sinusoidally stretch-activated Lethocerus muscles. Observed changes in X-ray reflections arising from myosin heads, actin filaments, troponin, and tropomyosin were consistent with the hypothesis that troponin bridges are the key agent of mechanical signal transduction. The time-resolved sequence of molecular changes suggests a mechanism for stretch activation, in which troponin bridges mechanically tug tropomyosin aside to relieve tropomyosin’s steric blocking of myosin–actin binding. This enables subsequent force production, with cross-bridge targeting further enhanced by stretch-induced lattice compression and thick-filament twisting. Similar linkages may operate in other muscle systems, such as mammalian cardiac muscle, where stretch activation is thought to aid in cardiac ejection.

subjectSciences (General)
general
0English
1National Acad Sciences
210.1073/pnas.1014599107
3PNAS (National Academy of Sciences)
4National Academy of Sciences (U.S.)
sourceidpnas_s
recordidpnas_s108_1_120
issn
00027-8424
100278424
21091-6490
310916490
rsrctypearticle
creationdate2011
addtitleProceedings of the National Academy of Sciences
searchscope
0pnas_full
1pnas4
2pnas5
scope
0pnas_full
1pnas4
2pnas5
lsr45$$EView_full_text_in_National_Academy_of_Sciences_(Access_to_full_text_may_be_restricted)
tmp01
0PNAS (National Academy of Sciences)
1National Academy of Sciences (U.S.)
tmp02
0PNE
1RNA
startdate20110104
enddate20110104
lsr40Proceedings of the National Academy of Sciences, 04 January 2011, Vol.108 (1), p.120
doi10.1073/pnas.1014599107
citationpf 120 vol 108 issue 1
lsr30VSR-Enriched:[pqid, galeid, pages]
sort
titleX-ray diffraction evidence for myosin-troponin connections and tropomyosin movement during stretch activation of insect flight muscle
authorRobert J. Perz-Edwards ; Thomas C. Irving ; Bruce A. J. Baumann ; David Gore ; Daniel C. Hutchinson ; Uroš Kržič ; Rebecca L. Porter ; Andrew B. Ward ; Michael K. Reedy
creationdate20110104
lso0120110104
facets
frbrgroupid8245147415525075733
frbrtype5
newrecords20190724
languageeng
topicSciences (General)
collection
0PNAS (National Academy of Sciences)
1National Academy of Sciences (U.S.)
prefilterarticles
rsrctypearticles
creatorcontrib
0Robert J. Perz-Edwards
1Thomas C. Irving
2Bruce A. J. Baumann
3David Gore
4Daniel C. Hutchinson
5Uroš Kržič
6Rebecca L. Porter
7Andrew B. Ward
8Michael K. Reedy
jtitleProceedings of the National Academy of Sciences
creationdate2011
toplevelpeer_reviewed
delivery
delcategoryRemote Search Resource
fulltextfulltext_linktorsrc
addata
au
0Robert J. Perz-Edwards
1Thomas C. Irving
2Bruce A. J. Baumann
3David Gore
4Daniel C. Hutchinson
5Uroš Kržič
6Rebecca L. Porter
7Andrew B. Ward
8Michael K. Reedy
atitleX-ray diffraction evidence for myosin-troponin connections and tropomyosin movement during stretch activation of insect flight muscle
jtitleProceedings of the National Academy of Sciences
risdate20110104
volume108
issue1
spage120
issn0027-8424
eissn1091-6490
formatjournal
genrearticle
ristypeJOUR
abstract

Stretch activation is important in the mechanical properties of vertebrate cardiac muscle and essential to the flight muscles of most insects. Despite decades of investigation, the underlying molecular mechanism of stretch activation is unknown. We investigated the role of recently observed connections between myosin and troponin, called “troponin bridges,” by analyzing real-time X-ray diffraction “movies” from sinusoidally stretch-activated Lethocerus muscles. Observed changes in X-ray reflections arising from myosin heads, actin filaments, troponin, and tropomyosin were consistent with the hypothesis that troponin bridges are the key agent of mechanical signal transduction. The time-resolved sequence of molecular changes suggests a mechanism for stretch activation, in which troponin bridges mechanically tug tropomyosin aside to relieve tropomyosin’s steric blocking of myosin–actin binding. This enables subsequent force production, with cross-bridge targeting further enhanced by stretch-induced lattice compression and thick-filament twisting. Similar linkages may operate in other muscle systems, such as mammalian cardiac muscle, where stretch activation is thought to aid in cardiac ejection.

pubNational Acad Sciences
doi10.1073/pnas.1014599107
urlhttp://www.pnas.org/content/108/1/120.abstract
lad01Proceedings of the National Academy of Sciences
pages120-125
date2011-01-04