Molecular dissection of the interaction of desmin with the C-terminal region of nebulin

Marie Louise Bang, Carol Gregorio, Siegfried Labeit

Research output: Contribution to journalArticle

62 Citations (Scopus)

Abstract

In vertebrate skeletal muscle, ultrastructural studies have suggested that the Z-line and extracellular intermediate filaments are linked, although a structural basis for this has remained elusive. We searched for potential novel ligands of the Z-line portion of nebulin by a yeast two-hybrid (Y2H) approach. This identified that the nebulin modules M160 to M170 interact with desmin. In desmin, deletion series experiments assigned a 19-kDa central coiled-coil domain as the nebulin-binding site. The specific interactions of nebulin and desmin were confirmed in vitro by GST pull-down experiments. In situ, the nebulin modules M176 to M181 colocalize with desmin in a Z-line-associated, striated pattern as shown by immunofluorescence studies. Our data are consistent with a model that desmin attaches directly to the Z-line through its interaction with the nebulin repeats M163-M170. This interaction may link myofibrillar Z-discs to the intermediate filament system, thereby forming a lateral linkage system which contributes to maintain adjacent Z-lines in register.

Original languageEnglish (US)
Pages (from-to)119-127
Number of pages9
JournalJournal of Structural Biology
Volume137
Issue number1-2
DOIs
StatePublished - 2002

Fingerprint

Desmin
Dissection
Intermediate Filaments
Fluorescent Antibody Technique
Vertebrates
nebulin
Skeletal Muscle
Yeasts
Binding Sites
Ligands

Keywords

  • Desmin
  • Myofibril architecture
  • Nebulin
  • Z-line

ASJC Scopus subject areas

  • Structural Biology

Cite this

Molecular dissection of the interaction of desmin with the C-terminal region of nebulin. / Bang, Marie Louise; Gregorio, Carol; Labeit, Siegfried.

In: Journal of Structural Biology, Vol. 137, No. 1-2, 2002, p. 119-127.

Research output: Contribution to journalArticle

@article{dd04f5f28f15458eb9e56cdb740a7607,
title = "Molecular dissection of the interaction of desmin with the C-terminal region of nebulin",
abstract = "In vertebrate skeletal muscle, ultrastructural studies have suggested that the Z-line and extracellular intermediate filaments are linked, although a structural basis for this has remained elusive. We searched for potential novel ligands of the Z-line portion of nebulin by a yeast two-hybrid (Y2H) approach. This identified that the nebulin modules M160 to M170 interact with desmin. In desmin, deletion series experiments assigned a 19-kDa central coiled-coil domain as the nebulin-binding site. The specific interactions of nebulin and desmin were confirmed in vitro by GST pull-down experiments. In situ, the nebulin modules M176 to M181 colocalize with desmin in a Z-line-associated, striated pattern as shown by immunofluorescence studies. Our data are consistent with a model that desmin attaches directly to the Z-line through its interaction with the nebulin repeats M163-M170. This interaction may link myofibrillar Z-discs to the intermediate filament system, thereby forming a lateral linkage system which contributes to maintain adjacent Z-lines in register.",
keywords = "Desmin, Myofibril architecture, Nebulin, Z-line",
author = "Bang, {Marie Louise} and Carol Gregorio and Siegfried Labeit",
year = "2002",
doi = "10.1006/jsbi.2002.4457",
language = "English (US)",
volume = "137",
pages = "119--127",
journal = "Journal of Structural Biology",
issn = "1047-8477",
publisher = "Academic Press Inc.",
number = "1-2",

}

TY - JOUR

T1 - Molecular dissection of the interaction of desmin with the C-terminal region of nebulin

AU - Bang, Marie Louise

AU - Gregorio, Carol

AU - Labeit, Siegfried

PY - 2002

Y1 - 2002

N2 - In vertebrate skeletal muscle, ultrastructural studies have suggested that the Z-line and extracellular intermediate filaments are linked, although a structural basis for this has remained elusive. We searched for potential novel ligands of the Z-line portion of nebulin by a yeast two-hybrid (Y2H) approach. This identified that the nebulin modules M160 to M170 interact with desmin. In desmin, deletion series experiments assigned a 19-kDa central coiled-coil domain as the nebulin-binding site. The specific interactions of nebulin and desmin were confirmed in vitro by GST pull-down experiments. In situ, the nebulin modules M176 to M181 colocalize with desmin in a Z-line-associated, striated pattern as shown by immunofluorescence studies. Our data are consistent with a model that desmin attaches directly to the Z-line through its interaction with the nebulin repeats M163-M170. This interaction may link myofibrillar Z-discs to the intermediate filament system, thereby forming a lateral linkage system which contributes to maintain adjacent Z-lines in register.

AB - In vertebrate skeletal muscle, ultrastructural studies have suggested that the Z-line and extracellular intermediate filaments are linked, although a structural basis for this has remained elusive. We searched for potential novel ligands of the Z-line portion of nebulin by a yeast two-hybrid (Y2H) approach. This identified that the nebulin modules M160 to M170 interact with desmin. In desmin, deletion series experiments assigned a 19-kDa central coiled-coil domain as the nebulin-binding site. The specific interactions of nebulin and desmin were confirmed in vitro by GST pull-down experiments. In situ, the nebulin modules M176 to M181 colocalize with desmin in a Z-line-associated, striated pattern as shown by immunofluorescence studies. Our data are consistent with a model that desmin attaches directly to the Z-line through its interaction with the nebulin repeats M163-M170. This interaction may link myofibrillar Z-discs to the intermediate filament system, thereby forming a lateral linkage system which contributes to maintain adjacent Z-lines in register.

KW - Desmin

KW - Myofibril architecture

KW - Nebulin

KW - Z-line

UR - http://www.scopus.com/inward/record.url?scp=18744397819&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=18744397819&partnerID=8YFLogxK

U2 - 10.1006/jsbi.2002.4457

DO - 10.1006/jsbi.2002.4457

M3 - Article

C2 - 12064939

AN - SCOPUS:18744397819

VL - 137

SP - 119

EP - 127

JO - Journal of Structural Biology

JF - Journal of Structural Biology

SN - 1047-8477

IS - 1-2

ER -