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Diversity of oligomerization in Drosophila semaphorins suggests a mechanism of functional fine-tuning

Abstract:

Semaphorin ligands and their plexin receptors are one of the major cell guidance factors that trigger localised changes in the cytoskeleton. Binding of semaphorin homodimer to plexin brings two plexins in close proximity which is a prerequisite for plexin signalling. This model appears to be too simplistic to explain the complexity and functional versatility of these molecules. Here, we determine crystal structures for all members of Drosophila class 1 and 2 semaphorins. Unlike previously rep...

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Publication status:
Accepted
Peer review status:
Peer reviewed

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Publisher copy:
10.1038/s41467-019-11683-y

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Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Biology
Role:
Author
More by this author
Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
NDM
Sub department:
Structural Biology
Role:
Author
More by this author
Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
NDM
Sub department:
Structural Biology
Role:
Author
More by this author
Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
NDM
Sub department:
Structural Biology
Role:
Author
More by this author
Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
NDM
Sub department:
Structural Biology
Role:
Author
More from this funder
Name:
Cancer Research UK
Grant:
17721
More from this funder
Name:
European Commission
Grant:
647278
More from this funder
Name:
Medical Research Council
Grant:
MR/M000141/1
Publisher:
Springer Nature
Journal:
Nature Communications More from this journal
Volume:
10
Issue:
2019
Article number:
3691
Publication date:
2019-08-15
Acceptance date:
2019-07-30
DOI:
ISSN:
2041-1723
Pubs id:
pubs:1036195
UUID:
uuid:0c16a563-d1ce-462d-b578-efbb47249886
Local pid:
pubs:1036195
Source identifiers:
1036195
Deposit date:
2019-07-30

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