These molecules orchestrate coordinated cytoskeletal reorganizations by generating different structures, like filopodium, lamellipodium
, or uropod, depending on the type of GTPase activated, that is, Cdc42, Rac, or RhoA, respectively .
Furthermore, single cell lamellipodium
formation, tail retraction, and directional movement may give clues as to what maybe impaired or enhanced in the cells of interest.
The perimeter of a lamellipodium
that expanded/retracted from its initial position during 100 sec period was traced using a freehand selection tool.
Our results firstly showed that antcin-H inhibited the Src/FAK/paxillin and Src/FAK/ERK-c-Fos-C/EBP-[beta] signaling pathways to impair lamellipodium
formation and decrease MMP-7 expression, consequently suppressing RCC cell migration and invasion, suggesting that antcin-H might have the potential for treating metastatic RCC.
Protrusion at the leading edge is driven by actin polymerization to form a lamellipodium
, which is a dynamic dendritic network with actin binding proteins such as Arp2/3 for nucleation and branching of actin filaments [22, 23], capping proteins for terminating actin polymerization  and ADF/cofilin for severing actin filaments .
Tamura, "The SH2-domian-containing inositol 5-phosphatase (SHIP)-2 binds to cMet directly via tyrosine residue 1356 and involves hepatocyte growth factor (HGF)-induced lamellipodium
formation, cell scattering and cell spreading," Oncogene, vol.
Higher magnification images showed that where a cell body or lamellipodium
contacted the surface, it was closely adherent and occluded the microcavities beneath .
Rottner, "The lamellipodium
: where motility begins," Trends in Cell Biology, vol.
Both Lyn-YFP and PH-Akt-GFP were found to co-localize in the lamellipodium
and phagocytic cup of PA infected MHS cells from live cell imaging studies.
Transverse arcs, instead, are curved stress fibers found parallel to the leading edge and are assembled from shorter actin filaments that originate in the lamellipodium
. They are contractile and do not attach to focal adhesions .
The leading edge is a thin, veil-like membranous structure called lamellipodium
that is filled with a dense, crisscrossed network of actin filaments (actin cytoskeleton).
Sea urchin coelomocytes undergo extensive actin-based retrograde flow, mediated in part by the Arp2/3 complexfacilitated polymerization of a dendritic brushwork of actin filaments in a wide lamellipodium
. In the present study we have experimented with changing this lamellipodial-based flow pattern into one that resembles the filopodial-dominated pattern present in neuronal growth cones.