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Proteomics Weekly


Researchers at Heidelberg University, Biochemistry Center publish new data on life sciences



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This article was published in Proteomics Weekly, which you can subscribe to online.

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2009 JUL 13 - (NewsRx.com) -- Scientists discuss in 'Reversible phosphorylation as a molecular switch to regulate plasma membrane targeting of acylated SH4 domain proteins' new findings in life sciences. According to recent research from Heidelberg, Germany, "Acylated SH4 domains represent N-terminal targeting signals that anchor peripheral membrane proteins such as Src kinases in the inner leaflet of plasma membranes. Here we provide evidence for a novel regulatory mechanism that may control the levels of SH4 proteins being associated with plasma membranes."

"Using a fusion protein of the SH4 domain of Leishmania HASPB and GFP as a model system, we demonstrate that threonine 6 is a substrate for phosphorylation. Substitution of threonine 6 by glutamate (to mimic a phosphothreonine residue) resulted in a dramatic redistribution from plasma membranes to intracellular sites with a particular accumulation in a perinuclear region. As shown by both pharmacological inhibition and RNAi-mediated down-regulation of the threonine/ serine-specific phosphatases PP1 and PP2A, recycling back to the plasma membrane required dephosphorylation of threonine 6," wrote S. Tournaviti and colleagues, Heidelberg University, Biochemistry Center.

The researchers concluded: "We provide evidence that a cycle of phosphorylation and dephosphorylation may also be involved in intracellular targeting of other SH4 proteins such as the Src kinase Yes."

Tournaviti and colleagues published their study in Traffic (Reversible phosphorylation as a molecular switch to regulate plasma membrane targeting of acylated SH4 domain proteins. Traffic, 2009;10(8):1047-60).

For additional information, contact S. Tournaviti, Heidelberg University Biochemistry Center, Heidelberg, Germany.

Publisher contact information for the journal Traffic is: Blackwell Publishing Inc., 350 Main St., Malden, MA 02148, USA.

Keywords: Germany, Heidelberg, Life Sciences, Proteomics. Fusion Proteins, Biochemistry, Cell Biology.

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

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