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© The Rockefeller University Press, 0021-9525/2000//1337 $5.00
The Journal of Cell Biology, Volume 148, Number 2, , 2000 1337-1338

© 2000 The Rockefeller University Press

We identified a 116-kD protein, termed p116^Rip, that binds to activated RhoA under two-hybrid conditions in yeast. Pull-down experiments in mouse N1E-115 neuroblastoma cells revealed an interaction between GST-RhoA and a protein of that comigrates with p116Rip and is recognized by anti–p116Rip antibody (Fig. 5 D). While this protein does not interact with GST alone, our recent experiments indicate that it is not p116^Rip but an unidentified bacterial protein that has the same apparent molecular size as p116^Rip and cross-reacts with the anti–p116^Rip antibody used. Therefore, the conclusion that p116^Rip interacts with RhoA in N1E-115 cells is premature.

Overexpression of p116^Rip in N1E-115 cells mimics dominant-negative RhoA in stimulating cell flattening and neurite outgrowth. We are currently characterizing p116^Rip in further biochemical detail and evaluating the relationship between p116^Rip and RhoA action.

We apologize for any additional work that our error may have caused other investigators.

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This Article Alert me when this article is cited Services Email this article Similar articles in this journal Alert me to new content in the JCB Download to citation manager Citing Articles Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                            What's this?