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Copeland, J. W.

Publications and source records attributed to Copeland, J. W..

2 recordsLinked to original sources

The formin FMNL2 plays a role in the response of melanoma cells to substrate stiffness

BackgroundCells are constantly sensing and responding to changes in their local environment to adapt their behaviour and morphology. These external stimuli include chemical and mechanical signals, and much recent work has revealed the complexity of the cellular response to changes in substrate stiffness. We investigated the effects of substrate stiffness on the morphology and motility of A2058 human melanoma cells. FMNL2, a formin protein associated with actin cytoskeleton dynamics, regulates cell morphology and motility but its role in stiffness sensing remains unclear. This study examines how A2058 cells respond to substrates of varying stiffness and evaluates the impact of FMNL2 depletion on these responses. ResultsWe found that with increasing substrate stiffness the cells transitioned from a rounded cell morphology to progressively more elongated morphologies with a concomitant increase in actin stress fiber alignment. Depletion of FMNL2 expression amplified these morphological changes, with knockdown cells showing consistently greater elongation and more pronounced stress fiber alignment compared to controls. Notably, the orientational order parameter (S) revealed higher alignment of actin filaments along the cells long axis in knockdown cells. Substrate stiffness also affected cell motility, indicated by an apparent optimal stiffness that maximized motility followed by a notable decrease in distance travelled during cell migration on progressively stiffer substrates. This decrease was largely attributable to a decrease in the time the cells spent in motion as the substrate stiffness increased. FMNL2 depletion significantly exacerbated this effect, with knockdown cells traveling shorter net distances and spending less time moving across all substrates. ConclusionsThis study demonstrates that substrate stiffness profoundly influences A2058 melanoma cell morphology and motility, with FMNL2 playing a pivotal regulatory role. Our observations suggest that FMNL2 is critical for maintaining motility and morphological adaptability under increased stiffness. Loss of FMNL2 enhanced stress fiber alignment and cell elongation while impairing motility, particularly on stiff substrates, revealing FMNL2 as a mechanosensitive effector. However, further biochemical work should be performed to determine the exact mechanisms by which FMNL2 participates in regulation of melanoma cell response to substrate stiffness.

cell biology↗

SPECC1L binds MYPT1/PP1β and can regulate its distribution between microtubules and filamentous actin

The subcellular localization, activity and substrate specificity of the serine/threonine protein phosphatase 1 catalytic subunit (PP1 cat) is mediated through its dynamic association with regulatory subunits in holoenzyme complexes. While some functional overlap is observed for the three human PP1cat isoforms, they also show distinct targeting based on relative preferences for specific regulatory subunits. A well-known example is the preferential association of MYPT1 with PP1{beta} in the myosin phosphatase complex. In smooth muscle, MYPT1/ PP1{beta} counteracts the muscle contraction induced by phosphorylation of the light chains of myosin by the myosin light chain kinase. This phosphatase complex is also found in non-muscle cells, where it is targeted to both myosin and non-myosin substrates and contributes to regulation of the balance of cytoskeletal structure and motility during cell migration and division. Although it remains unclear how MYPT1/PP1{beta} traffics between microtubule- and actin-associated substrates, our identification of the microtubule- and actin-binding protein SPECC1L in both the PP1{beta} and MYPT1 interactomes suggested that it may be the missing link. Validation of their association, together with the strong overlap that we observed for the SPECC1L and MYPT1 interactomes, suggested that they exist in a stable complex in the cell. We further showed that SPECC1L binds MYPT1 directly, and that it can impact the balance of the distribution of the MYPT1/ PP1{beta} complex between the microtubule and filamentous actin networks.

cell biology↗