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First published online January 14, 2005

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New profile for profilin

Profilins are small ubiquitous proteins that regulate cytoplasmic actin dynamics. They also bind to several nuclear proteins but the significance of these interactions is unclear. Marcell Lederer, Brigitte Jockusch and Martin Rothkegel now identify a new profilin ligand in a yeast two-hybrid screen (see p. 331). p42^POP - a hitherto unknown Myb-related transcription factor - contains one functional tryptophan cluster motif in its DNA-binding domain, an acidic domain, nuclear import and export signals, a leucine zipper, and a proline cluster that mediates profilin binding. p42^POP, which is widely expressed in mouse tissues, acts as a repressor of transcription in luciferase assays; this activity is altered by interaction with profilin. Profilin and p42^POP coprecipitate in vitro and, more importantly, they interact in vivo in both the cytoplasmic and nuclear compartments. Further biochemical, cell biological and genetic analyses are now needed, suggest the authors, to determine exactly how profilin regulates gene transcription and, more generally, how microfilament dynamics are linked to signal transduction.

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Related articles in JCS:

Profilin regulates the activity of p42^POP, a novel Myb-related transcription factor

Marcell Lederer, Brigitte M. Jockusch, and Martin Rothkegel
JCS 2005 118: 331-341. [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?