Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

Splice variants of the Drosophila PS2 integrins differentially interact with the extracellular ligands Tiggrin, D-laminin alpha 2 and Ten-m.

Graner, Michael W. ; Bunch, Thomas A. ; Baumgartner, Stefan LU orcid ; Kerschen, Arthur and Brower, Danny L. (1998) In Journal of Biological Chemistry 273(29). p.18235-18241
Abstract
Two new potential ligands of theDrosophila PS2 integrins have been characterized by functional interaction in cell culture. These potential ligands are a new Drosophila laminin α2 chain encoded by the wing blister locus and Ten-m, an extracellular protein known to be involved in embryonic pattern formation. As with previously identified PS2 ligands, both contain RGD sequences, and RGD-containing fragments of these two proteins (DLAM-RGD and TENM-RGD) can support PS2 integrin-mediated cell spreading. In all cases, this spreading is inhibited specifically by short RGD-containing peptides. As previously found for the PS2 ligand tiggrin (and the tiggrin fragment TIG-RGD), TENM-RGD induces maximal spreading of cells expressing integrin... (More)
Two new potential ligands of theDrosophila PS2 integrins have been characterized by functional interaction in cell culture. These potential ligands are a new Drosophila laminin α2 chain encoded by the wing blister locus and Ten-m, an extracellular protein known to be involved in embryonic pattern formation. As with previously identified PS2 ligands, both contain RGD sequences, and RGD-containing fragments of these two proteins (DLAM-RGD and TENM-RGD) can support PS2 integrin-mediated cell spreading. In all cases, this spreading is inhibited specifically by short RGD-containing peptides. As previously found for the PS2 ligand tiggrin (and the tiggrin fragment TIG-RGD), TENM-RGD induces maximal spreading of cells expressing integrin containing the αPS2C splice variant. This is in contrast to DLAM-RGD, which is the first Drosophila polypeptide shown to interact preferentially with cells expressing the αPS2 m8 splice variant. The βPS integrin subunit also varies in the presumed ligand binding region as a result of alternative splicing. For TIG-RGD and TENM-RGD, the β splice variant has little effect, but for DLAM-RGD, maximal cell spreading is supported only by the βPS4A form of the protein. Thus, the diversity in PS2 integrins due to splicing variations, in combination with diversity of matrix ligands, can greatly enhance the functional complexity of PS2-ligand interactions in the developing animal. The data also suggest that the splice variants may alter regions of the subunits that are directly involved in ligand interactions, and this is discussed with respect to models of integrin structure. (Less)
Please use this url to cite or link to this publication:
author
; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
273
issue
29
pages
18235 - 18241
publisher
American Society for Biochemistry and Molecular Biology
ISSN
1083-351X
language
English
LU publication?
yes
id
9e4e453e-9a01-42b7-b3db-e1fec66667b6
alternative location
https://www.sciencedirect.com/science/article/pii/S0021925818804215?via%3Dihub
date added to LUP
2022-07-26 15:33:54
date last changed
2022-07-27 08:14:07
@article{9e4e453e-9a01-42b7-b3db-e1fec66667b6,
  abstract     = {{Two new potential ligands of theDrosophila PS2 integrins have been characterized by functional interaction in cell culture. These potential ligands are a new Drosophila laminin α2 chain encoded by the wing blister locus and Ten-m, an extracellular protein known to be involved in embryonic pattern formation. As with previously identified PS2 ligands, both contain RGD sequences, and RGD-containing fragments of these two proteins (DLAM-RGD and TENM-RGD) can support PS2 integrin-mediated cell spreading. In all cases, this spreading is inhibited specifically by short RGD-containing peptides. As previously found for the PS2 ligand tiggrin (and the tiggrin fragment TIG-RGD), TENM-RGD induces maximal spreading of cells expressing integrin containing the αPS2C splice variant. This is in contrast to DLAM-RGD, which is the first Drosophila polypeptide shown to interact preferentially with cells expressing the αPS2 m8 splice variant. The βPS integrin subunit also varies in the presumed ligand binding region as a result of alternative splicing. For TIG-RGD and TENM-RGD, the β splice variant has little effect, but for DLAM-RGD, maximal cell spreading is supported only by the βPS4A form of the protein. Thus, the diversity in PS2 integrins due to splicing variations, in combination with diversity of matrix ligands, can greatly enhance the functional complexity of PS2-ligand interactions in the developing animal. The data also suggest that the splice variants may alter regions of the subunits that are directly involved in ligand interactions, and this is discussed with respect to models of integrin structure.}},
  author       = {{Graner, Michael W. and Bunch, Thomas A. and Baumgartner, Stefan and Kerschen, Arthur and Brower, Danny L.}},
  issn         = {{1083-351X}},
  language     = {{eng}},
  number       = {{29}},
  pages        = {{18235--18241}},
  publisher    = {{American Society for Biochemistry and Molecular Biology}},
  series       = {{Journal of Biological Chemistry}},
  title        = {{Splice variants of the Drosophila PS2 integrins differentially interact with the extracellular ligands Tiggrin, D-laminin alpha 2 and Ten-m.}},
  url          = {{https://www.sciencedirect.com/science/article/pii/S0021925818804215?via%3Dihub}},
  volume       = {{273}},
  year         = {{1998}},
}