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Increasing spatial resolution of photoregulated GTPases through immobilized peripheral membrane proteins.

ABSTRACT: Light-induced dimerizing systems, e.g. iLID, are an increasingly utilized optogenetics tool to perturb cellular signaling. The major benefit of this technique is that it allows external spatiotemporal control over protein localization with sub-cellular specificity. However, when it comes to local recruitment of signaling components to the plasmamembrane, this precision in localization is easily lost due to rapid diffusion of the membrane anchor. In this study, we explore different approaches of countering the diffusion of peripheral membrane anchors, to the point where we detect immobilized fractions with iFRAP on a timescale of several minutes. One method involves simultaneous binding of the membrane anchor to a secondary structure, the microtubules. The other strategy utilizes clustering of the anchor into large immobile structures, which can also be interlinked by employing tandem recruitable domains. For both approaches, the anchors are peripheral membrane constructs, which also makes them suitable for in vitro use. Upon combining these slower diffusing anchors with recruitable guanine exchange factors (GEFs), we show that we can elicit much more localized morphological responses from Rac1 and Cdc42 as compared to a regular CAAX-box based membrane anchor in living cells. Thanks to these new slow diffusing anchors, more precisely defined membrane recruitment experiments are now possible.

SUBMITTER: Van Geel O

PROVIDER: S-EPMC7549704 | biostudies-literature |

REPOSITORIES: biostudies-literature

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Project description:Continental- and regional-scale assessments of gaps in protected area networks typically use relatively coarse range maps for well documented species groups, creating uncertainty about the fate of unexamined biodiversity and providing insufficient guidance for land managers. By building habitat suitability models for a taxonomically diverse group of 2216 imperiled plants and animals, we revealed comprehensive and detailed protection opportunities in the conterminous United States. Summing protection-weighted range-size rarity (PWRSR, the product of the percent of modeled habitat outside of protected areas and the inverse of modeled habitat extent) uncovered novel patterns of biodiversity importance. Concentrations of unprotected imperiled species in places such as the northern Sierra Nevada, central and northern Arizona, the Rocky Mountains of Utah and Colorado, southeastern Texas, southwestern Arkansas, and Florida's Lake Wales Ridge have rarely if ever been featured in continental- and regional-scale analyses. Inclusion of diverse taxa (vertebrates, freshwater mussels, crayfishes, bumble bees, butterflies, skippers, and vascular plants) partially drove these new patterns. When analyses were restricted to groups typically included in previous studies (birds, mammals, and amphibians), up to 53% of imperiled species in other groups were left out. The finer resolution of modeled inputs (990 m) also resulted in a more geographically dispersed pattern. For example, 90% of the human population of the conterminous United States lives within 50 km of modeled habitat for one or more species with high PWRSR scores. Over one-half of the habitat for 818 species occurs within federally lands managed for biodiversity protection; an additional 360 species have over one-half of their modeled habitat on federal multiple use land. Freshwater animals occur in places with poorer landscape condition but with less exposure to climate change than other groups, suggesting that habitat restoration is an important conservation strategy for these species. The results provide fine-scale, taxonomically diverse inputs for local and regional priority-setting and show that although protection efforts are still widely needed on private lands, notable gains can be achieved by increasing protection status on selected federal lands.

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Increasing spatial resolution of photoregulated GTPases through immobilized peripheral membrane proteins.

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