Journal
CYTOSKELETON
Volume 70, Issue 3, Pages 161-177Publisher
WILEY-BLACKWELL
DOI: 10.1002/cm.21097
Keywords
single fluorescent-molecule imaging; tracking; PIX; diffusion; archipelago architecture; percolation
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Funding
- Japan Society for the Promotion of Science (JSPS)
- Ministry of Education, Culture, Science and Technology (MEXT) of the Japanese government
- World Premier International Research Center Initiative by MEXT, Japan
- Grants-in-Aid for Scientific Research [23657101, 11F01796] Funding Source: KAKEN
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The focal adhesion (FA) is an integrin-based structure built in/on the plasma membrane (PM), linking the extracellular matrix to the actin stress-fibers, working as cell migration scaffolds. Previously, we proposed the archipelago architecture of the FA, in which FA largely consists of fluid membrane, dotted with small islands accumulating FA proteins: membrane molecules enter the inter-island channels in the FA zone rather freely, and the integrins in the FA-protein islands rapidly exchanges with those in the bulk membrane. Here, we examined how Rac1, a small G-protein regulating FA formation, and its activators PIX and PIX, are recruited to the FA zones. PIX molecules are recruited from the cytoplasm to the FA zones directly. In contrast, majorities of Rac1 molecules first arrive from the cytoplasm on the general inner PM surface, and then enter the FA zones via lateral diffusion on the PM, which is possible due to rapid Rac1 diffusion even within the FA zones, slowed only by a factor of two to four compared with that outside. The constitutively-active Rac1 mutant exhibited temporary and all-time immobilizations in the FA zone, suggesting that upon PIX-induced Rac1 activation at the FA-protein islands, Rac1 tends to be immobilized at the FA-protein islands. (c) 2013 Wiley Periodicals, Inc
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