Actin, a ATPase superfamily protein regulates some vital biological functions like cell locomotion, cytokinesis, synaptic plasticity, and cell signalling in higher eukaryotes are dependent on the dynamics of actin polymerization process. Impaired regulation of actin polymerization has been implicated in the...
Myosin belong to a superfamily that consists of different types of ‘motor proteins that are very important in the concentration of muscle. This particular type of protein refers to as ATP-dependent and it is responsible for actin-based motility. It is mainly applied in describing a particular g...
Myosin V is an actin-activated ATPase, a type of motor protein representing the fifth of 13 classes of unconventional myosins (for reviews seeMooseker 1993;Hammer 1994;Mooseker & Cheney 1995;Hasson & Mooseker 1996, 1997b;Titus 1997a;Baker & Titus 1998). The first group of myosin V membe...
Kinesins are a superfamily of motors that drive microtubule-based transport in cells. There are many kinesins in pollen, but their functions are largely unknown23. In worms, rice, and moss, kinesins have been reported to be required for the nuclear migration process in somatic cells27,28,29...
While the subunit composition of these families varies, they all assemble around a catalytic subunit defined by the presence of a conserved helicase superfamily 2 (SF2) ATPase domain4, 5. The ATPase domain consists of two recA-like subdomains, with the nucleotide-binding and DNA-binding sites ...
Although myosin superfamily members share this domain structure, it is thought that each myosin has its unique motility activity that is closely related to its physiological function. For instance, some myosin family members, such as myosin V, are suitable for cargo transportation, whereas others ...
cells expressing the GFP-MYA2-head6IQ indicated that the functionless motor protein inhibits endogenous myosins. Furthermore, co-expression of the GFP-MYA2-head6IQ with other F-actin markers disrupted its attachment to F-actin. In nuclei, the GFP-myosin associated with short bundles of F-...
In addition, mutations may disrupt the interaction between actin and ABPs that regulate its function, affecting processes like filament branching, bundling, capping, severing, and the interaction with myosin motors [[23, 157]]. This disruption in actin structure and function can result in abnormal...
To test whether the stiffness-dependent differential traction still exists in the absence of myosin-II activity, we treated the cells with 20 µM of blebbistatin (BBS), a myosin ATPase inhibitor46,47for 1 hour after plating the cells for 3 hours, and measured the traction of the ce...
TM9SF4 is a membrane protein with nine transmembrane domains and a long hydrophilic N-terminus with a signal peptide10. Previous studies reported that TM9SF can be cleaved to form a ~30 kDa N-terminal fragment (NTF)18. To confirm this, several TM9SF4 constructs containing different tags wer...