Ghent University Academic Bibliography

Advanced

Interaction of α-catulin with dystrobrevin contributes to integrity of dystrophin complex in muscle

Hyun J Oh, Linu S Abraham, Jolanda van Hengel UGent, Christophe Stove UGent, Tomasz J Proszynski, Kris Gevaert UGent, Joseph X DiMario, Joshua R Sanes, Frans Van Roy UGent and Hongkyun Kim (2012) JOURNAL OF BIOLOGICAL CHEMISTRY. 287(26). p.21717-21728
abstract
The dystrophin complex is a multimolecular membrane-associated protein complex whose defects underlie many forms of muscular dystrophy. The dystrophin complex is postulated to function as a structural element that stabilizes the cell membrane by linking the contractile apparatus to the extracellular matrix. Abetter understanding of how this complex is organized and localized will improve our knowledge of the pathogenic mechanisms of diseases that involve the dystrophin complex. In a Caenorhabditis elegans genetic study, we demonstrate that CTN-1/alpha-catulin, a cytoskeletal protein, physically interacts with DYB-1/alpha-dystrobrevin (a component of the dystrophin complex) and that this interaction is critical for the localization of the dystrophin complex near dense bodies, structures analogous to mammalian costameres. We further show that in mouse alpha-catulin is localized at the sarcolemma and neuromuscular junctions and interacts with alpha-dystrobrevin and that the level of alpha-catulin is reduced in alpha-dystrobrevin- deficient mouse muscle. Intriguingly, in the skeletal muscle of mdx mice lacking dystrophin, we discover that the expression of alpha-catulin is increased, suggesting a compensatory role of alpha-catulin in dystrophic muscle. Together, our study demonstrates that the interaction between alpha-catulin and alpha-dystrobrevin is evolutionarily conserved in C. elegans and mammalian muscles and strongly suggests that this interaction contributes to the integrity of the dystrophin complex.
Please use this url to cite or link to this publication:
author
organization
alternative title
Interaction of alpha-catulin with dystrobrevin contributes to integrity of dystrophin complex in muscle
year
type
journalArticle (original)
publication status
published
subject
keyword
GLYCOPROTEIN COMPLEX, MDX MICE, BK CHANNEL, PROTEIN COMPLEX, SKELETAL-MUSCLE, MUSCULAR-DYSTROPHIES, NEMATODE CAENORHABDITIS-ELEGANS, C. ELEGANS, LOCALIZATION, PATHOGENESIS
journal title
JOURNAL OF BIOLOGICAL CHEMISTRY
J. Biol. Chem.
volume
287
issue
26
pages
21717 - 21728
Web of Science type
Article
Web of Science id
000306418600013
JCR category
BIOCHEMISTRY & MOLECULAR BIOLOGY
JCR impact factor
4.651 (2012)
JCR rank
61/288 (2012)
JCR quartile
1 (2012)
ISSN
0021-9258
DOI
10.1074/jbc.M112.369496
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
2970055
handle
http://hdl.handle.net/1854/LU-2970055
date created
2012-08-09 09:12:16
date last changed
2012-08-09 10:57:08
@article{2970055,
  abstract     = {The dystrophin complex is a multimolecular membrane-associated protein complex whose defects underlie many forms of muscular dystrophy. The dystrophin complex is postulated to function as a structural element that stabilizes the cell membrane by linking the contractile apparatus to the extracellular matrix. Abetter understanding of how this complex is organized and localized will improve our knowledge of the pathogenic mechanisms of diseases that involve the dystrophin complex. In a Caenorhabditis elegans genetic study, we demonstrate that CTN-1/alpha-catulin, a cytoskeletal protein, physically interacts with DYB-1/alpha-dystrobrevin (a component of the dystrophin complex) and that this interaction is critical for the localization of the dystrophin complex near dense bodies, structures analogous to mammalian costameres. We further show that in mouse alpha-catulin is localized at the sarcolemma and neuromuscular junctions and interacts with alpha-dystrobrevin and that the level of alpha-catulin is reduced in alpha-dystrobrevin- deficient mouse muscle. Intriguingly, in the skeletal muscle of mdx mice lacking dystrophin, we discover that the expression of alpha-catulin is increased, suggesting a compensatory role of alpha-catulin in dystrophic muscle. Together, our study demonstrates that the interaction between alpha-catulin and alpha-dystrobrevin is evolutionarily conserved in C. elegans and mammalian muscles and strongly suggests that this interaction contributes to the integrity of the dystrophin complex.},
  author       = {Oh, Hyun J and Abraham, Linu S and van Hengel, Jolanda and Stove, Christophe and Proszynski, Tomasz J and Gevaert, Kris and DiMario, Joseph X and Sanes, Joshua R and Van Roy, Frans and Kim, Hongkyun},
  issn         = {0021-9258},
  journal      = {JOURNAL OF BIOLOGICAL CHEMISTRY},
  keyword      = {GLYCOPROTEIN COMPLEX,MDX MICE,BK CHANNEL,PROTEIN COMPLEX,SKELETAL-MUSCLE,MUSCULAR-DYSTROPHIES,NEMATODE CAENORHABDITIS-ELEGANS,C. ELEGANS,LOCALIZATION,PATHOGENESIS},
  language     = {eng},
  number       = {26},
  pages        = {21717--21728},
  title        = {Interaction of \ensuremath{\alpha}-catulin with dystrobrevin contributes to integrity of dystrophin complex in muscle},
  url          = {http://dx.doi.org/10.1074/jbc.M112.369496},
  volume       = {287},
  year         = {2012},
}

Chicago
Oh, Hyun J, Linu S Abraham, Jolanda van Hengel, Christophe Stove, Tomasz J Proszynski, Kris Gevaert, Joseph X DiMario, Joshua R Sanes, Frans Van Roy, and Hongkyun Kim. 2012. “Interaction of Α-catulin with Dystrobrevin Contributes to Integrity of Dystrophin Complex in Muscle.” Journal of Biological Chemistry 287 (26): 21717–21728.
APA
Oh, H. J., Abraham, L. S., van Hengel, J., Stove, C., Proszynski, T. J., Gevaert, K., DiMario, J. X., et al. (2012). Interaction of α-catulin with dystrobrevin contributes to integrity of dystrophin complex in muscle. JOURNAL OF BIOLOGICAL CHEMISTRY, 287(26), 21717–21728.
Vancouver
1.
Oh HJ, Abraham LS, van Hengel J, Stove C, Proszynski TJ, Gevaert K, et al. Interaction of α-catulin with dystrobrevin contributes to integrity of dystrophin complex in muscle. JOURNAL OF BIOLOGICAL CHEMISTRY. 2012;287(26):21717–28.
MLA
Oh, Hyun J, Linu S Abraham, Jolanda van Hengel, et al. “Interaction of Α-catulin with Dystrobrevin Contributes to Integrity of Dystrophin Complex in Muscle.” JOURNAL OF BIOLOGICAL CHEMISTRY 287.26 (2012): 21717–21728. Print.