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First published online October 12, 2006

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A new player in patterning by proteolysis

The transition from egg to embryo in C. elegans involves fertilisation, meiosis, exit from meiosis and the establishment of the anteroposterior (AP) axis. These last two processes may be connected - many mutants with meiotic defects, including several that affect ubiquitin-mediated proteolysis, have polarity defects. Now, Bruce Bowerman and colleagues report that PAM-1, a puromycin-sensitive aminopeptidase that might act in conjunction with the proteasome to degrade ubiquitin-tagged proteins, is required for both meiotic exit and AP polarity in one-cell worm embryos (see p. 4281). The researchers show that meiotic exit is delayed and the AP axis is not specified in pam-1 mutants. As inactivation of the B-type cyclin CYB-3 rescues the first (but not the second) of these defects, PAM-1 may regulate CYB-3 during meiotic exit but presumably targets other proteins to regulate polarity. The researchers conclude that PAM-1 contributes to the proteolytic machinery that triggers cell-cycle progression and the establishment of AP polarity in the early worm embryo, and possibly in other embryos.

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The puromycin-sensitive aminopeptidase PAM-1 is required for meiotic exit and anteroposterior polarity in the one-cell Caenorhabditis elegans embryo

Rebecca Lyczak, Lynnsey Zweier, Thomas Group, Mary Ann Murrow, Christine Snyder, Lindsay Kulovitz, Alexander Beatty, Kristen Smith, and Bruce Bowerman
Development 2006 133: 4281-4292. [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 Development 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?