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Centralspindlin, a complex composed of the subunits ZEN-4 and CYK-4, recruits and regulates proteins that modulate the actin cytoskeleton to promote cleavage furrow formation and progression during cytokinesis.
It is tempting to speculate that NleL, NleG and Tir may work together to modulate the actin pedestal formation.
The ability of CRMP4 to modulate the actin cytoskeleton raises the possibility that CRMP4 plays an additional role in regulating actomyosin-based events during mitosis.
EphB-dependent regulation of dendritic filopodia motility and spine formation relies on forward signaling through guanine nucleotide exchange factors (GEFs) and other downstream molecules such as p21 activated kinase (PAK) that modulate the actin cytoskeleton [14], [17], [24], [25], [26].
Different regulatory systems modulate the actin responses during chemotaxis.
There are other proteins that bind to Tir and modulate the actin cytoskeleton, such as IQGAP1.
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In addition, α-actinins associate with ion channels such as the L-type calcium channel and the Kv1.4 and Kv1.5 potassium channels influencing the activation of ion channels and intracellular Ca2+ levels, which modulate the actin-binding properties of α-actinins [16].
O-GlcNAcylation of actin may modulate the actin-tropomyosin interaction and be involved in the polymerization of myosin heavy chains [ 24].
Moreover, it has been recognized that caldesmon and TM can modulate the actin-myosin interaction in a cooperative manner [ 20], suggesting that functional effects of these proteins on actin-myosin coupling and smooth muscle mechanics ought to be interpreted in parallel.
These pathways include modulating the actin cytoskeleton, mediating signaling by Rho family GTPases and calmodulin, regulating E-cadherin and β-catenin function and organizing microtubules.
In the normal lung cells, Slit2 binds to Robo1 and activates downstream molecules, modulating the actin cytoskeleton and inhibiting cell migration.
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