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Differential expression of Dystroglycan-spliceforms with and without the mucin-like domain during Drosophila embryogenesis

Schneider, Martina LU and Baumgartner, Stefan LU (2008) In Fly 2(1). p.29-35
Abstract
Dystroglycan (DG) is a widely expressed extracellular matrix (ECM) receptor required for muscle viability, synaptogenesis, basement-membrane formation and epithelial development. As an integral component of the Dystrophin-associated glycoprotein complex, DG plays a central role in linking the ECM and the cytoskeleton. Disruption of this linkage in skeletal muscle is the underlying cause in various types of muscular dystrophies (MD). One particular type of MD is caused by alterations of O-linked glycosylation in the mucin-like domain of DG, which is required for binding of the ECM molecules Laminin and Perlecan. In epithelial cells, reduced expression of DG is associated with increased invasiveness of cancer cells and loss of cell polarity.... (More)
Dystroglycan (DG) is a widely expressed extracellular matrix (ECM) receptor required for muscle viability, synaptogenesis, basement-membrane formation and epithelial development. As an integral component of the Dystrophin-associated glycoprotein complex, DG plays a central role in linking the ECM and the cytoskeleton. Disruption of this linkage in skeletal muscle is the underlying cause in various types of muscular dystrophies (MD). One particular type of MD is caused by alterations of O-linked glycosylation in the mucin-like domain of DG, which is required for binding of the ECM molecules Laminin and Perlecan. In epithelial cells, reduced expression of DG is associated with increased invasiveness of cancer cells and loss of cell polarity. Drosophila Dg is, in contrast to vertebrate Dg, subjected to differential splicing of the mRNA. Interestingly, the shorter DG splice forms lack the mucin-like domain. Here, we describe the embryonic expression patterns of full-length DG and a short variant of DG. We find that differential splicing of Dg is developmentally regulated and tissue-specific. In some tissues, e. g., hindgut, midgut constrictions, gonads, both DG variants can be detected. For the long form, we detected specific expression at the blastoderm stage, in the epidermis and in the tracheal pits. The short form showed exclusive expression in dorsal vessel cells, chordotonal organs and dorsal median cells. In the nervous system, the long form is predominantly expressed on axons, while the short form is present on glial cells. Our findings further support the idea that DG forms lacking the mucin-like domain serve a specific function in Drosophila. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
differential splicing, pattern, expression, embryogenesis, mucin-like domain, Drosophila, dystroglycan
in
Fly
volume
2
issue
1
pages
29 - 35
publisher
Landes Bioscience
external identifiers
  • wos:000256387100003
  • pmid:18820475
  • scopus:77956502084
ISSN
1933-6934
language
English
LU publication?
yes
id
ad455513-6439-4d74-9c98-4b96378b3055 (old id 1201758)
alternative location
http://www.landesbioscience.com/journals/fly/article/SchneiderFLY2-1.pdf
http://www.ncbi.nlm.nih.gov/pubmed/18820475?dopt=Abstract
date added to LUP
2008-09-16 13:40:00
date last changed
2017-02-05 03:30:30
@article{ad455513-6439-4d74-9c98-4b96378b3055,
  abstract     = {Dystroglycan (DG) is a widely expressed extracellular matrix (ECM) receptor required for muscle viability, synaptogenesis, basement-membrane formation and epithelial development. As an integral component of the Dystrophin-associated glycoprotein complex, DG plays a central role in linking the ECM and the cytoskeleton. Disruption of this linkage in skeletal muscle is the underlying cause in various types of muscular dystrophies (MD). One particular type of MD is caused by alterations of O-linked glycosylation in the mucin-like domain of DG, which is required for binding of the ECM molecules Laminin and Perlecan. In epithelial cells, reduced expression of DG is associated with increased invasiveness of cancer cells and loss of cell polarity. Drosophila Dg is, in contrast to vertebrate Dg, subjected to differential splicing of the mRNA. Interestingly, the shorter DG splice forms lack the mucin-like domain. Here, we describe the embryonic expression patterns of full-length DG and a short variant of DG. We find that differential splicing of Dg is developmentally regulated and tissue-specific. In some tissues, e. g., hindgut, midgut constrictions, gonads, both DG variants can be detected. For the long form, we detected specific expression at the blastoderm stage, in the epidermis and in the tracheal pits. The short form showed exclusive expression in dorsal vessel cells, chordotonal organs and dorsal median cells. In the nervous system, the long form is predominantly expressed on axons, while the short form is present on glial cells. Our findings further support the idea that DG forms lacking the mucin-like domain serve a specific function in Drosophila.},
  author       = {Schneider, Martina and Baumgartner, Stefan},
  issn         = {1933-6934},
  keyword      = {differential splicing,pattern,expression,embryogenesis,mucin-like domain,Drosophila,dystroglycan},
  language     = {eng},
  number       = {1},
  pages        = {29--35},
  publisher    = {Landes Bioscience},
  series       = {Fly},
  title        = {Differential expression of Dystroglycan-spliceforms with and without the mucin-like domain during Drosophila embryogenesis},
  volume       = {2},
  year         = {2008},
}