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First published online February 22, 2006

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-tubulin on death row

Cytotoxic T-cells (CTLs) kill virus-infected cells and tumour cells by releasing granules containing proteins that induce apoptosis. One of these - granzyme B - is thought to act by cleaving caspases, critical apoptotic enzymes whose cleavage activates the death program. Granzyme B can kill cells even when caspases are inhibited, however, and so it must have other targets. Chris Bleackley and co-workers now reveal that one of these is the cytoskeleton (see p. 858). They have analysed cell lysates treated with granzyme B by mass spectrometry and identify -tubulin as one of the proteins cleaved. Moreover, they show that -tubulin is cleaved in vivo in cells undergoing CTL-induced apoptosis and that this can be blocked by inhibiting granzyme B activity (but not caspases). Bleackley and co-workers have pinned down the cleavage site to an aspartate residue (D38) in a C-terminal sequence that is highly conserved among tubulin isoforms. Since this region binds to proteins that regulate microtubule dynamics and the cleaved -tubulin partitions predominantly into the soluble pool, the authors propose that an important apoptotic effect of granzyme B is microtubule disassembly.

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Related articles in JCS:

Identification of -tubulin as a granzyme B substrate during CTL-mediated apoptosis

Ing Swie Goping, Tracy Sawchuk, D. Alan Underhill, and R. Chris Bleackley
JCS 2006 119: 858-865. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?