TY - JOUR
T1 - Proteasomal degradation resolves competition between cell polarization and cellular wound healing
AU - Kono, Keiko
AU - Saeki, Yasushi
AU - Yoshida, Satoshi
AU - Tanaka, Keiji
AU - Pellman, David
N1 - Funding Information:
We thank D. Finley and M. Springer for critical reading of the manuscript; C. Mann, W. Guo, M. Cyert, L. Hicke, and D. Lew for reagents; Z. Shi for pilot experiments; S. Gygi and R. Tomaino for mass spectrometry analysis; L. Cameron for advice on microscopy; members of the Pellman lab, especially S. Buttery and B. Atkins, for helpful discussions; and C. Kuroda for strain construction. This work was supported by NIH grant RO1 GM061345.
PY - 2012/7/6
Y1 - 2012/7/6
N2 - Cellular wound healing, enabling the repair of membrane damage, is ubiquitous in eukaryotes. One aspect of the wound healing response is the redirection of a polarized cytoskeleton and the secretory machinery to the damage site. Although there has been recent progress in identifying conserved proteins involved in wound healing, the mechanisms linking these components into a coherent response are not defined. Using laser damage in budding yeast, we demonstrate that local cell wall/membrane damage triggers the dispersal of proteins from the site of polarized growth, enabling their accumulation at the wound. We define a protein-kinase-C-dependent mechanism that mediates the destruction of the formin Bni1 and the exocyst component Sec3. This degradation is essential to prevent competition between the site of polarized growth and the wound. Mechanisms to overcome competition from a pre-existing polarized cytoskeleton may be a general feature of effective wound healing in polarized cells.
AB - Cellular wound healing, enabling the repair of membrane damage, is ubiquitous in eukaryotes. One aspect of the wound healing response is the redirection of a polarized cytoskeleton and the secretory machinery to the damage site. Although there has been recent progress in identifying conserved proteins involved in wound healing, the mechanisms linking these components into a coherent response are not defined. Using laser damage in budding yeast, we demonstrate that local cell wall/membrane damage triggers the dispersal of proteins from the site of polarized growth, enabling their accumulation at the wound. We define a protein-kinase-C-dependent mechanism that mediates the destruction of the formin Bni1 and the exocyst component Sec3. This degradation is essential to prevent competition between the site of polarized growth and the wound. Mechanisms to overcome competition from a pre-existing polarized cytoskeleton may be a general feature of effective wound healing in polarized cells.
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U2 - 10.1016/j.cell.2012.05.030
DO - 10.1016/j.cell.2012.05.030
M3 - Article
C2 - 22727045
AN - SCOPUS:84863615537
SN - 0092-8674
VL - 150
SP - 151
EP - 164
JO - Cell
JF - Cell
IS - 1
ER -