Final answer:
Actin-binding proteins in cells have different functions. Thymosin sequesters actin monomers, ARP binds to actin filaments, and Formin and Gelsolin proteins are involved in the formation of actin structures. Rho GTPases regulate actin cytoskeleton changes.
Step-by-step explanation:
There are several actin-binding proteins in cells that have different functions. Some proteins like thymosin bind to actin monomers and sequester them until needed for the formation of filaments. Other proteins like ARP bind to the ends of actin filaments. The Formin family of proteins are important for nucleation of branched actin structures in lamellipodia of moving cells, while Gelsolin proteins are important for the formation of unbranched actin filaments found in filopodia.
Proteins belonging to the Rho family of GTPases regulate changes in the actin cytoskeleton in response to extracellular signals.
The blanks in the provided sentences should be filled with 'thymosin', 'capping', 'ARP', 'lamellipodia', 'formin', 'filopodia', and 'Rho' to describe functions of different actin-binding proteins and their roles in cell motility and cytoskeleton changes.
For each of the following sentences, fill in the blanks with the best word or phrase selected from the list below:
Some proteins such as thymosin bind to actin monomers, sequestering them until needed for filament formation.
Capping proteins bind to the end of actin filaments.
The ARP proteins are important for nucleation of the branched actin structures commonly found in the lamellipodia of moving cells,
whereas formin proteins are important for the formation of unbranched actin filaments commonly found in filopodia.
Proteins belonging to the Rho family of GTPases regulate changes in the actin cytoskeleton in response to extracellular signals.