Myosin II
- Colocation of Tpm3.1 and myosin IIa heads defines a discrete subdomain in stress fibres
Summary: Super-resolution and electron microscopy are used to show that tropomyosin Tpm3.1 is periodically distributed along stress fibres and linked to the organisation of myosin II motors.
- Contractility kits promote assembly of the mechanoresponsive cytoskeletal network
Summary: Cytosolic complexes of myosin II, cortexillin I and IQGAPs define the assembly and feedback mechanisms of a mechanoresponsive contractility controller.
- Parallel assembly of actin and tropomyosin, but not myosin II, during de novo actin filament formation in live mice
Summary: De novo assembly of functional actin–tropomyosin filaments in live rodents is investigated. Unlike non-muscle myosin II, tropomyosin is added to the actin filament shortly after nucleation.
- Steric hindrance in the upper 50 kDa domain of the motor Myo2p leads to cytokinesis defects in fission yeast
Summary: An unbiased genetic screen uncovers a mutation that reverses a steric clash in the myosin II motor head, which was previously reported to cause defective actomyosin ring-dependent cytokinesis in fission yeast.
- Myosin II governs collective cell migration behaviour downstream of guidance receptor signalling
Summary: Non-muscle myosin II (NMII) is the key regulator for the control of border cell behaviours. Positively regulated by EGFR, NMII induces the switch of border cell movement from linear to rotational.
- TOR complex 2 localises to the cytokinetic actomyosin ring and controls the fidelity of cytokinesis
Highlighted Article: A role for the TOR signalling pathway in regulating cytokinesis is identified. This myosin-dependent mechanism modulates the stability of the S. pombe CapZ complex to regulate actin function.
- The contractome – a systems view of actomyosin contractility in non-muscle cells
Summary: A systematic analysis of the non-muscle myosin II literature reveals the multitude of cellular processes in which contractility plays a role and the complex protein interaction network regulating it.