1
This cell is a good model to study the possible function(s) of f-actin in signal transduction processes.
2
Lattice light-sheet and structured illumination microscopy reveal a proximal leading process nanoscale architecture wherein f-actin and drebrin intervene between microtubules and the plasma membrane.
3
In this report we have studied the ability of these proteins to interact with other components of membrane skeleton such as ankyrin, f-actin and calmodulin.
4
In addition, cortactin-A was able to bind along the side of F-actin.
5
Staining of F-actin revealed differential spatial and temporal patterns of several muscles.
6
Recruitment occurs in the absence of F-actin, but ring formation is delayed.
7
However, esculetin induced redistribution of F-actin accompanied by increased cell adhesion and size.
8
This latter response was dictated by stress through focal-adhesion-induced reorganization of F-actin filaments.
9
Furthermore, a peptide containing the coiled-coil sequence only was sufficient for F-actin binding.
10
Pharmacological analysis indicated that RIC1 affected F-actin dynamics in pollen tubes.
11
The effect on cell motility was also visualized by fluorescence staining of F-Actin.
12
The F-actin-independent fraction was visualized as cortical dots in the absence of F-actin.
13
SSH1 co-localizes with F-actin and accumulates onto the cleavage furrow and the midbody.
14
Spatiotemporal reorganization of F-actin at the IS is inhibited in PKCδ-interfered T lymphocytes.
15
Maintenance of F-actin turnover is essential for plant cell morphogenesis.
16
These results indicate that nexilin is a novel F-actin-binding protein localized at cell-matrix AJ.