7-days of FREE Audio papers, translation & more with Prime
7-days of FREE Prime access
7-days of FREE Audio papers, translation & more with Prime
7-days of FREE Prime access
https://doi.org/10.21236/ada410349
Copy DOIPublication Date: Aug 1, 2002 |
Abstract : Cdc42p and other proteins polarize to a cap at the presumptive bud site and the tip of the bud. The observation that Cdc42p polarizes in the complete absence of F-actin has been confirmed repeatedly. These studies used LatA as a method to completely depolymerize actin, and suggested that Cdc42p polarization is actin-independent. Polarized secretion and endocytic uptake require F-actin cables and patches, respectively. When LatA is applied to yeast cells neither actin patches nor cables are detectable, disrupting all F-actin-dependent processes. Thus, Cdc42p polarization occurs by a non-secretory pathway. Is the polarized cap static? Current models of Cdc42p function propose that the cap is an organizing center for polarity. Since it is associated with the plasma membrane, the cap may be static, acting as a polymerization site for actin cables by formins, assembly of septins, signal transduction, etc. Our data indicate that the cap is, in reality, dynamic. We show that the loss of actin cables, but not actin patches, leads to Cdc42p delocalization. We propose that the initial polarization of Cdc42p is an actin-independent process; continued polarization is the result of two competing processes: endocytic removal of the plasma membrane, and a deposition process, dependent on polarized secretion.
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.