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  4. Analysis of the S. pombe signalling scaffold protein Cdc11p reveals an essential role for the N-terminal domain in SIN signalling
 
research article

Analysis of the S. pombe signalling scaffold protein Cdc11p reveals an essential role for the N-terminal domain in SIN signalling

Krapp, A.  
•
Cano, E.
•
Simanis, V.  
2004
FEBS Letters

The initiation of cytokinesis in the fission yeast Schizosaccharomyces pombe is signalled by the septation initiation network (SIN). Signalling originates from the spindle pole body (SPB), where SIN proteins are anchored by a scaffold composed of cdc11p and sid4p. Cdc11p links the other SIN proteins to sid4p and the SPB. Homologues of cdc11p have been identified in Saccharomyes cerevisiae (Nud1p) and human cells (Centriolin). We have defined functional domains of cdc11p by analysis of deletion mutants. We demonstrate that the C-terminal end of cdc11p is necessary for SPB localisation. We also show that the N-terminal domain is necessary and sufficient for signal transduction, since tethering of this domain to the SPB will substitute for cdc11p in SIN function.

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Type
research article
DOI
10.1016/j.febslet.2004.03.098
Author(s)
Krapp, A.  
Cano, E.
Simanis, V.  
Date Issued

2004

Published in
FEBS Letters
Volume

565

Issue

1-3

Start page

176

End page

80

Subjects

Cell Cycle Proteins/chemistry/*physiology

•

Cell Division

•

Cytoskeletal Proteins/chemistry/*physiology

•

Deoxyribonucleases/metabolism

•

Drosophila Proteins/metabolism

•

Gene Deletion

•

Green Fluorescent Proteins

•

Luminescent Proteins/metabolism

•

Mitotic Spindle Apparatus

•

Mutation

•

Phosphorylation

•

Protein Structure

•

Tertiary

•

Protein-Serine-Threonine Kinases/metabolism

•

Saccharomyces cerevisiae

•

Saccharomyces cerevisiae Proteins/chemistry/metabolism/*physiology

•

Schizosaccharomyces/*metabolism

•

*Signal Transduction

•

Temperature

Editorial or Peer reviewed

REVIEWED

Written at

EPFL

EPFL units
UPSIM  
Available on Infoscience
October 21, 2008
Use this identifier to reference this record
https://infoscience.epfl.ch/handle/20.500.14299/30363
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