Topography and structural diversity regulate ecosystem multifunctionality in a subtropical evergreen broad-leaved forest

Forest functionality is generally considered a byproduct of forest diversity. Perhaps unsurprisingly, many researchers associate increasing multi-functionality with increasing diversity. Diversity, however, is an often-overused word that may describe a host of features, including the diversity of species, functional trait and structure. Furthermore, variable environmental features (such as topography) influence the interaction between forest plants and their function. Incorporating complex topography (like that associated with tropical and subtropical forests) into estimates of forest functionality is challenging and highly uncertain. In this paper, we applied structural equation models to disentangle the relative importance of topography and different components of what might be considered “plant diversity” to forest multifunctionality using repeated census of a 20-ha subtropical forest plot. We found that multifunctionality was principally influenced by structural diversity more so than either species composition or functional trait diversity. In our SEM model approach, we observed variations in topography could account for about 30% of variation in multifunctionality. Furthermore, variations in topography could indirectly influence forest multifunctionality by changing species composition, functional trait diversity, and structural diversity. Our work highlights the importance of topography and forest structure in regulating subtropical forest multifunctionality on the local scale. This suggests future subtropical forest management should focus on regulating forest structure. Namely, our results suggest land managers must take topography (and the complex interaction between topography and plant diversity) into account in order to build robust and multifunctional forests

KDEL Receptor Trafficking to the Plasma Membrane Is Regulated by ACBD3 and Rab4A-GTP

KDEL receptor-1 maintains homeostasis in the early secretory pathway by capturing and retrieving ER chaperones to the ER during heavy secretory activity. Unexpectedly, a fraction of the receptor is also known to reside in the plasma membrane (PM), although it is largely unknown exactly how the KDEL receptor gets exported from the Golgi and travels to the PM. We have previously shown that a Golgi scaffolding protein (ACBD3) facilitates KDEL receptor localization at the Golgi via the regulating cargo wave-induced cAMP/PKA-dependent signaling pathway. Upon endocytosis, surface-expressed KDEL receptor undergoes highly complex itineraries through the Golgi and the endo-lysosomal compartments, where the endocytosed receptor utilizes Rab14A- and Rab11A-positive recycling endosomes and clathrin-decorated tubulovesicular carriers. In this study, we sought to investigate the mechanism through which the KDEL receptor gets exported from the Golgi en route to the PM. We report here that ACBD3 depletion results in greatly increased trafficking of KDEL receptor to the PM via Rab4A-positive tubular carriers emanating from the Golgi. Expression of constitutively activated Rab4A mutant (Q72L) increases the surface expression of KDEL receptor up to 2~3-fold, whereas Rab4A knockdown or the expression of GDP-locked Rab4A mutant (S27N) inhibits KDEL receptor targeting of the PM. Importantly, KDELR trafficking from the Golgi to the PM is independent of PKA- and Src kinase-mediated mechanisms. Taken together, these results reveal that ACBD3 and Rab4A play a key role in regulating KDEL receptor trafficking to the cell surface

Stretchable strain sensors with dentate groove structure for enhanced sensing recoverability

Stretchable strain sensors based on conductive polymer composites commonly utilize elastic polymers as the matrix. However, elastic polymers always show strong mechanical hysteresis effect leading to shoulder peak phenomenon and thereby poor recoverability of strain sensors. Herein, we design a stretchable rough filament strain sensor with dentate groove structure to eliminate the shoulder peak phenomenon and improve recoverability. The filament strain sensor is fabricated by the extrusion of poly(styrene-b-ethylene-b-butylene-b-styrene) (SEBS) filament constructing dentate groove structure and the subsequent ultrasonic treatment decorating carbon nanotubes (CNTs) on the surface of the SEBS filament. It is interesting to find that the strain sensing range of rough SEBS/CNTs filaments with dentate groove structure is wider than that of smooth filaments. More importantly, the rough filament strain sensors exhibit significantly enhanced recoverability without shoulder peak during the releasing process while the rough dentate groove structure has minor effects on the mechanical properties of SEBS filaments. The great improvement is ascribed to the uniform distribution of deformation because of the dentate groove structure, which induces reduction of the mechanical hysteresis effect and thereby decreases residual strain. Moreover, the rough filament strain sensors have a favorable integration of good stability, fast response time of 300 ms (0.5% strain is applied with a high strain rate of 500 mm/min) and excellent durability (1976 cycles at the strain of 50%). The rough filament strain sensors can accurately and stably monitor both large and subtle human motions (such as body motion, expression and phonation), showing broad application prospects in wearable devices

Crosstalk between KDEL receptor and EGF receptor mediates cell proliferation and migration via STAT3 signaling

Abstract Hostile microenvironment of cancer cells provoke a stressful condition for endoplasmic reticulum (ER) and stimulate the expression and secretion of ER chaperones, leading to tumorigenic effects. However, the molecular mechanism underlying these effects is largely unknown. In this study, we reveal that the last four residues of ER chaperones, which are recognized by KDEL receptor (KDELR), is required for cell proliferation and migration induced by secreted chaperones. By combining proximity-based mass spectrometry analysis, split venus imaging and membrane yeast two hybrid assay, we present that EGF receptor (EGFR) may be a co-receptor for KDELR on the surface. Prior to ligand addition, KDELR spontaneously oligomerizes and constantly undergoes recycling near the plasma membrane. Upon KDEL ligand binding, the interactions of KDELR with itself and with EGFR increase rapidly, leading to augmented internalization of KDELR and tyrosine phosphorylation in the C-terminus of EGFR. STAT3, which binds the phosphorylated tyrosine motif on EGFR, is subsequently activated by EGFR and mediates cell growth and migration. Taken together, our results suggest that KDELR serves as a bona fide cell surface receptor for secreted ER chaperones and transactivates EGFR-STAT3 signaling pathway

ACBD3 modulates KDEL receptor interaction with PKA for its trafficking via tubulovesicular carrier

Background KDEL receptor helps establish cellular equilibrium in the early secretory pathway by recycling leaked ER-chaperones to the ER during secretion of newly synthesized proteins. Studies have also shown that KDEL receptor may function as a signaling protein that orchestrates membrane flux through the secretory pathway. We have recently shown that KDEL receptor is also a cell surface receptor, which undergoes highly complex itinerary between trans-Golgi network and the plasma membranes via clathrin-mediated transport carriers. Ironically, however, it is still largely unknown how KDEL receptor is distributed to the Golgi at steady state, since its initial discovery in late 1980s. Results We used a proximity-based in vivo tagging strategy to further dissect mechanisms of KDEL receptor trafficking. Our new results reveal that ACBD3 may be a key protein that regulates KDEL receptor trafficking via modulation of Arf1-dependent tubule formation. We demonstrate that ACBD3 directly interact with KDEL receptor and form a functionally distinct protein complex in ArfGAPs-independent manner. Depletion of ACBD3 results in re-localization of KDEL receptor to the ER by inducing accelerated retrograde trafficking of KDEL receptor. Importantly, this is caused by specifically altering KDEL receptor interaction with Protein Kinase A and Arf1/ArfGAP1, eventually leading to increased Arf1-GTP-dependent tubular carrier formation at the Golgi. Conclusions These results suggest that ACBD3 may function as a negative regulator of PKA activity on KDEL receptor, thereby restricting its retrograde trafficking in the absence of KDEL ligand binding. Since ACBD3 was originally identified as PAP7, a PBR/PKA-interacting protein at the Golgi/mitochondria, we propose that Golgi-localization of KDEL receptor is likely to be controlled by its interaction with ACBD3/PKA complex at steady state, providing a novel insight for establishment of cellular homeostasis in the early secretory pathway

Facile Fabrication of PEDOT:PSS‐Based Free‐Standing Conducting Film for Highly Efficient Electromagnetic Interference Shielding

Abstract With the growing popularity of portable and wearable smart electronics, the electromagnetic shielding materials with high shielding effectiveness (SE) as well as light weight and excellent mechanical strength are in high. In this work, the PEDOT:PSS‐based free‐standing conducting film with superior conductivity and mechanical strength is prepared through a facile fabrication. The cellulose nanofibers (CNFs) are first introduced to induce an orderly grow and stack of the PEDOT grains. A phosphoric acid immersion process is then employed to remove the insulating CNF and PSS in the film. The obtained free‐standing conducting film shows a record conductivity of 3508 S cm−1 and its elongation at break reaches 3.75%. Encouragingly, the film delivers an excellent electromagnetic interference (EMI) shielding behavior with a SE of 49 dB in the X‐band (8.2–12.4 GHz) at a thickness of 4 µm. The superior conductivity, mechanical strength, and high SE as well as its facile solution processability make this free‐standing conducting film to be an attractive EMI material for portable and wearable smart electronics