Here, we investigate the mechanical properties
of actin bundles in the absence of cross-linkers.
Not exact matches
Actin allows vital actions to be performed by assembling and disassembling itself spontaneously, continually and rapidly in the form
of filaments that organize themselves and form networks
of parallel
bundles or intertwined meshes (known as lamellar networks).
Generation
of contractile actomyosin
bundles depends on mechanosensitive
actin filament assembly and disassembly.
The switch - associated protein 70 (SWAP - 70)
bundles actin filaments and contributes to the regulation
of F -
actin dynamics.
Platelet - activating factor - induced clathrin - mediated endocytosis requires β - arrestin - 1 recruitment and activation
of the p38 MAPK signalosome at the plasma membrane for
actin bundle formation.
By use
of purified proteins, a small number
of components are sufficient for the assembly
of filopodia - like
bundles: WASP - coated beads,
actin, Arp2 / 3 complex, and fascin.
Beads coated with Arp2 / 3 - activating proteins can induce two distinct types
of actin organization in cytoplasmic extracts: (1) comet tails or clouds displaying a dendritic array
of actin filaments and (2) stars with filament
bundles radiating from the bead.
We propose that fascin is a key specific
actin cross-linker, providing stiffness for filopodial
bundles, and that its dynamic behavior allows for efficient coordination between elongation and
bundling of filopodial
actin filaments.
RNA interference
of fascin reduced the number
of filopodia, and remaining filopodia had abnormal morphology with wavy and loosely
bundled actin organization.
On the basis
of analysis
of this system, we proposed a model for filopodial formation in which
actin filaments
of a preexisting dendritic network are elongated by inhibition
of capping and subsequently cross-linked into
bundles by fascin.
While absent from normal epithelia, an
actin bundling protein, fascin, becomes expressed in invasive carcinoma
of different origins.