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Bioinformatics Advance Access originally published online on March 16, 2009
Bioinformatics 2009 25(10):1219-1222; doi:10.1093/bioinformatics/btp151
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© The Author 2009. Published by Oxford University Press. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org

A concanavalin A-like lectin domain in the CHS1/LYST protein, shared by members of the BEACH family

Agathe Burgess 1, Jean-Paul Mornon 2, Geneviève de Saint-Basile 1 and Isabelle Callebaut 2,*

1INSERM, U768; Université René Descartes-Paris 5; Hôpital Necker-Enfants Malades, 149 rue de Sèvres 75015, Paris, F-75015 and 2Université Pierre et Marie Curie-Paris 6, IMPMC-UMR7590, Paris, F-75005; CNRS, Paris, F-75016; Université Paris Diderot-Paris 7, Paris, F-75013, France

*To whom correspondence should be addressed.


  Abstract

CHS1/LYST, the causative protein of the Chediak–Higashi syndrome (CHS), belongs to the BEACH (named after BEige And Chediak–Higashi) family, which includes various large proteins sharing the same C-terminal domain architecture [a PH (Pleckstrin homology)–BEACH domain followed by WD repeats). Members of the BEACH family are generally defined as vesicle-trafficking regulatory proteins, but their functions remain to be determined at the molecular level.

Here, using a panel of sensitive methods of sequence analysis, we show that the N-terminal regions of BEACH proteins contain an as yet not described domain, which shares striking similarities with clostridial neurotoxins and defines a novel family within the concanavalin A (ConA)-like lectin superfamily. These results suggest that the BEACH ConA-like lectin domain could be involved in oligosaccharide binding associated with protein traffic and sorting along the secretory pathway, especially in relation with components of the vesicle fusion machinery.

Contact: isabelle.callebaut{at}impmc.jussieu.fr

Supplementary information: Supplementary data are available at Bioinformatics online.

Associate Editor: Alex Bateman

Received on January 6, 2009; revised on March 11, 2009; accepted on March 13, 2009

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