Probing the integrin-actin linkage using high-resolution protein velocity mapping
0301 basic medicine
Cytoplasm
Integrins
Green Fluorescent Proteins
3T3 Cells
CHO Cells
Models, Biological
Actins
Cytoskeletal Proteins
Luminescent Proteins
Mice
03 medical and health sciences
Cricetulus
Cricetinae
Image Interpretation, Computer-Assisted
Protein Interaction Mapping
Cell Adhesion
Image Processing, Computer-Assisted
Animals
Algorithms
Cells, Cultured
Cytoskeleton
DOI:
10.1242/jcs.03321
Publication Date:
2006-12-11T22:44:32Z
AUTHORS (7)
ABSTRACT
Cell migration is regulated in part by the connection between the substratum and the actin cytoskeleton. However, the very large number of proteins involved in this linkage and their complex network of interactions make it difficult to assess their role in cell migration. We apply a novel image analysis tool, spatio-temporal image correlation spectroscopy (STICS), to quantify the directed movements of adhesion-related proteins and actin in protrusions of migrating cells. The STICS technique reveals protein dynamics even when protein densities are very low or very high, and works in the presence of large, static molecular complexes. Detailed protein velocity maps for actin and the adhesion-related proteins α-actinin, α5-integrin, talin, paxillin, vinculin and focal adhesion kinase are presented. The data show that there are differences in the efficiency of the linkage between integrin and actin among different cell types and on the same cell type grown on different substrate densities. We identify potential mechanisms that regulate efficiency of the linkage, or clutch, and identify two likely points of disconnect, one at the integrin and the other at α-actinin or actin. The data suggests that the efficiency of the linkage increases as actin and adhesions become more organized showing the importance of factors that regulate the efficiency in adhesion signaling and dynamics.
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