Proteomics Weekly

Researchers at University of Glasgow have published new data on fusion proteins

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"Understanding the conserved mechanisms by which SM proteins function in this process has proved challenging, largely due to an apparent lack of conservation of binding mechanisms between different SM-syntaxin pairs. In the present study, we have identified a hitherto uncharacterized mode of binding between syntaxin 4 and Munc18c that is independent of the binding mode shown previously to utilize the N-terminal peptide of syntaxin 4. Our data demonstrate that syntaxin 4 and Munc18c interact via two distinct modes of binding, analogous to those employed by syntaxin 1a-Munc18a and syntaxin 16-Vps45p (vacuolar protein sorting 45)," wrote V. Aran and colleagues, University of Glasgow.

The researchers concluded: "These data support the notion that all syntaxin/SM proteins bind using conserved mechanisms, and pave the way for the formulation of unifying hypotheses of SM protein function.."

Aran and colleagues published their study in Biochemical Journal (Characterization of two distinct binding modes between syntaxin 4 and Munc18c. Biochemical Journal, 2009;419(Part 3):655-660).

For additional information, contact N.J. Bryant, University of Glasgow, Faculty Biomedical & Life Science, Division Molecular & Cellular Biology, Henry Wellcome Laboratory Cell Biology, Davidson Bldg, Glasgow G12 8QQ, Lanark, Scotland.

Publisher contact information for the Biochemical Journal is: Portland Press Ltd., Third Floor, Eagle House, 16 Procter Street, London WC1V 6 Nx, England.

Keywords: Scotland, Biochemical, N Ethylmaleimide, Proteomics. Fusion Proteins, Therapy, Treatment, University of Glasgow.

This article was prepared by Proteomics Weekly editors from staff and other reports. Copyright 2009, Proteomics Weekly via NewsRx.com.