wing blister, A new Drosophila laminin alpha chain required for cell adhesion and migration during embryonic and imaginal development
Martin, Doris ; Zusman, Susan ; Li, Xitong ; Williams, Erin L. ; Khare, Narmada LU ; DaRocha, Sol ; Chiquet-Ehrismann, Ruth and Baumgartner, Stefan LU
(1999)
In Journal of Cell Biology
145(1).
p.191-201
- Abstract
We report the molecular and functional characterization of a new α chain of laminin in Drosophila. The new laminin chain appears to be the Drosophila counterpart of both vertebrate α2 (also called merosin) and α1 chains, with a slightly higher degree of homology to α2, suggesting that this chain is an ancestral version of both αl and α2 chains. During embryogenesis, the protein is associated with basement membranes of the digestive system and muscle attachment sites, and during larval stage it is found in a specific pattern in wing and eye discs. The gene is assigned to a locus called wing blister (wb), which is essential for embryonic viability. Embryonic phenotypes include twisted germbands and fewer pericardial cells, resulting in... (More)
We report the molecular and functional characterization of a new α chain of laminin in Drosophila. The new laminin chain appears to be the Drosophila counterpart of both vertebrate α2 (also called merosin) and α1 chains, with a slightly higher degree of homology to α2, suggesting that this chain is an ancestral version of both αl and α2 chains. During embryogenesis, the protein is associated with basement membranes of the digestive system and muscle attachment sites, and during larval stage it is found in a specific pattern in wing and eye discs. The gene is assigned to a locus called wing blister (wb), which is essential for embryonic viability. Embryonic phenotypes include twisted germbands and fewer pericardial cells, resulting in gaps in the presumptive heart and tracheal trunks, and myotubes detached from their target muscle attachment sites. Most phenotypes are in common with those observed in Drosophila laminin α3, 5 mutant embryos and many are in common with those observed in integrin mutations. Adult phenotypes show blisters in the wings in viable allelic combinations, similar to phenotypes observed in integrin genes. Mutation analysis in the eye demonstrates a function in rhabdomere organization. In summary, this new laminin α chain is essential for embryonic viability and is involved in processes requiring cell migration and cell adhesion.
(Less)
- author
- Martin, Doris
; Zusman, Susan
; Li, Xitong
; Williams, Erin L.
; Khare, Narmada
LU
; DaRocha, Sol
; Chiquet-Ehrismann, Ruth
and Baumgartner, Stefan
LU
- organization
- publishing date
- 1999-04-05
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Development, Drosophila, Extracellular matrix, Laminin, wing blister
- in
- Journal of Cell Biology
- volume
- 145
- issue
- 1
- pages
- 191 - 201
- publisher
- Rockefeller University Press
- external identifiers
-
- pmid:10189378
- scopus:0033526047
- ISSN
- 0021-9525
- DOI
- 10.1083/jcb.145.1.191
- language
- English
- LU publication?
- yes
- id
- b2407a46-9a27-4fd1-bc01-584dde933d4f
- date added to LUP
- 2019-05-21 14:05:31
- date last changed
- 2024-04-02 03:46:09
@article{b2407a46-9a27-4fd1-bc01-584dde933d4f,
abstract = {{<p>We report the molecular and functional characterization of a new α chain of laminin in Drosophila. The new laminin chain appears to be the Drosophila counterpart of both vertebrate α2 (also called merosin) and α1 chains, with a slightly higher degree of homology to α2, suggesting that this chain is an ancestral version of both αl and α2 chains. During embryogenesis, the protein is associated with basement membranes of the digestive system and muscle attachment sites, and during larval stage it is found in a specific pattern in wing and eye discs. The gene is assigned to a locus called wing blister (wb), which is essential for embryonic viability. Embryonic phenotypes include twisted germbands and fewer pericardial cells, resulting in gaps in the presumptive heart and tracheal trunks, and myotubes detached from their target muscle attachment sites. Most phenotypes are in common with those observed in Drosophila laminin α3, 5 mutant embryos and many are in common with those observed in integrin mutations. Adult phenotypes show blisters in the wings in viable allelic combinations, similar to phenotypes observed in integrin genes. Mutation analysis in the eye demonstrates a function in rhabdomere organization. In summary, this new laminin α chain is essential for embryonic viability and is involved in processes requiring cell migration and cell adhesion.</p>}},
author = {{Martin, Doris and Zusman, Susan and Li, Xitong and Williams, Erin L. and Khare, Narmada and DaRocha, Sol and Chiquet-Ehrismann, Ruth and Baumgartner, Stefan}},
issn = {{0021-9525}},
keywords = {{Development; Drosophila; Extracellular matrix; Laminin; wing blister}},
language = {{eng}},
month = {{04}},
number = {{1}},
pages = {{191--201}},
publisher = {{Rockefeller University Press}},
series = {{Journal of Cell Biology}},
title = {{wing blister, A new Drosophila laminin alpha chain required for cell adhesion and migration during embryonic and imaginal development}},
url = {{http://dx.doi.org/10.1083/jcb.145.1.191}},
doi = {{10.1083/jcb.145.1.191}},
volume = {{145}},
year = {{1999}},
}