English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Reception of Slit requires only the chondroitin–sulphate-modified extracellular domain of Syndecan at the target cell surface.

Chanana, B., Steigemann, P., Jäckle, H., & Vorbrüggen, G. (2009). Reception of Slit requires only the chondroitin–sulphate-modified extracellular domain of Syndecan at the target cell surface. Proceedings of the National Academy of Sciences of the United States of America, 106(29), 11984-11988. doi:10.1073/pnas.0901148106.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-D7E8-8 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-7EA0-8
Genre: Journal Article

Files

show Files
hide Files
:
588032.pdf (Publisher version), 2MB
Name:
588032.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
588032-Suppl.pdf (Supplementary material), 933KB
Name:
588032-Suppl.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Description:
-

Creators

show
hide
 Creators:
Chanana, B.1, Author              
Steigemann, P.1, Author              
Jäckle, H.1, Author              
Vorbrüggen, G.2, Author              
Affiliations:
1Department of Molecular Developmental Biology, MPI for biophysical chemistry, Max Planck Society, ou_578590              
2Research Group of Molecular Cell Dynamics, MPI for biophysical chemistry, Max Planck Society, ou_578593              

Content

show
hide
Free keywords: Drosophila; heparan sulfate; Slit signal transduction; axon guidance
 Abstract: Syndecan (Sdc) is a conserved transmembrane heparan sulfate proteoglycan (HSPG) bearing additional chondroitin sulfate (CS) modifications on its extracellular domain. In vertebrates, this extracellular domain of Sdc is shed and acts as a soluble effector of cellular communication events, and its cytoplasmic domain participates in intracellular signaling needed to maintain epithelial integrity. In Drosophila, Sdc has been shown to be necessary for Slit signaling-dependent axon and myotube guidance during CNS development and muscle pattern formation. We report that Sdc acts in a cell-autonomous manner in Slit-receiving cells and that its membrane-anchored extracellular domain is sufficient to mediate Slit signaling. Sdc activity can be replaced by the human homolog hsdc2. However, the HSPG Dally-like protein (Dlp), which lacks CS modifications at its extracellular domain, can only partially substitute for Sdc function, and its activity is not restricted to the Slit target cells. Our results suggest that Sdc and Dlp act in a cooperative but nonredundant fashion in axon and myotube guidance. We propose that Dlp, which lacks CS modifications, participates in the transfer of Slit from its site of expression to the target cells, where CS-modified Sdc concentrates and presents the ligand.

Details

show
hide
Language(s): eng - English
 Dates: 2009-07-21
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: eDoc: 436126
DOI: 10.1073/pnas.0901148106
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Proceedings of the National Academy of Sciences of the United States of America
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 106 (29) Sequence Number: - Start / End Page: 11984 - 11988 Identifier: -