In modern coexistence theory, species coexistence can either arise via stabilizing mechanisms that increase niche differences or equalizing mechanisms that reduce fitness differences.Having a common currency for interpreting these mechanisms is essential for synthesizing knowledge across different studies and systems.Several methods for quantifying niche and fitness differences exist, but it remains unknown to what extent these methods agree on the reasons why species coexist. Here, we apply four common methods to quantify niche and fitness differences to one simulated and two empirical data sets. We ask if different methods result in different insights into what drives species coexistence.
We find that different methods disagree on the effects of resource supply rates (simulated data), and of plant traits or phylogenetic distance (empirical data), on niche and fitness differences. More specifically, these methods often do not agree better than expected by chance. We argue for (1) a better understanding of what connects and sets apart different methods, and (2) the simultaneous application of multiple methods to enhance a more complete insight into why species coexist.
Plexins are semaphorin receptors that play essential roles in neuronal axon guidance and in many other important biological processes. Plexin signaling depends on a semaphorin-induced dimerization mechanism, and is modulated by small signaling GTPases of the Rho family, of which RND1 serves as a plexin activator yet its close homolog RhoD an inhibitor. Using molecular dynamics (MD) simulations we showed that RND1 reinforces plexin dimerization interface whereas RhoD destabilizes it due to their differential interaction with cell membrane. Upon binding plexin dimers at the Rho-GTPase binding (RBD) domains, RND1 and RhoD interact differently with the inner leaflet of cell membrane, and exert opposite effects on the dimerization interface via an allosteric network involving the RBD domain, RBD linkers, and a buttress segment adjacent to the dimerization interface. The differential membrane interaction is attributed to the fact that, unlike RND1, RhoD features a short C-terminal tail and a positively-charged membrane interface.
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