Synthetic molecule blocks exit from cell organelle

70652986 — Mon, 26 Mar 2007 05:43:14 -0400

The ubiquitous, small GTPases are a family of signal transduction molecules that play crucial roles in numerous biological processes, including cell motility and division. Though scientists have eyed these proteins as potential therapeutic targets for years, inhibitors of GTPases have proven exceedingly difficult to develop; currently there are only a handful in existence. But in a Nov. 20, 2005 advanced online publication in Nature Chemical Biology,Tom Kirchhausen, Matthew Shair, and Henry Pelish have revealed a new class of GTPase inhibitor. They have synthesized secramine, a small molecule that blocks the GTPase Cdc42, which is crucial for vesicular transport and cell migration. The finding provides a new means to study protein traffic from the Golgi apparatus and offers hope that unique and specific GTPase inhibitors might one day be used to treat disease.

Matthew Shair imitates, improves on nature

70652986 — Mon, 26 Mar 2007 05:26:28 -0400

Matthew Shair and his students work in "protein trafficking." Genes in living cells carry instructions for making proteins essential to life. These proteins have to get from place to place in the cells and to destinations outside the cells. It's like traffic on a busy freeway. The problem Shair set for himself was to find traffic "cops." The process of searching for them should lead to new discoveries about basic biology. In addition, molecules found to perturb protein traffficking can be involved in disease. Studying them could be the first step in finding better treatments. Using biomimetic synthesis, two graduate students, Henry Pelish and Nick Westwood, made a library of about 3,000 molecules that they guessed might be the types that cause protein traffic jams.

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Synthetic molecule blocks exit from cell organelle

Matthew Shair imitates, improves on nature