Reconstruction induced by external environment (such as applied voltage bias and test electrolytes) changes catalyst component and catalytic behaviors. Investigations of complete reconstruction in energy conversion recently receive intensive attention, which promote the targeted design of top‐performance materials with maximum component utilization and good stability. However, the advantages of complete reconstruction, its design strategies, and extensive applications have not achieved the profound understandings and summaries it deserves. Here, this review systematically summarizes several important advances in complete reconstruction for the first time, which includes 1) fundamental understandings of complete reconstruction, the characteristics and advantages of completely reconstructed catalysts, and their design principles, 2) types of reconstruction‐involved precatalysts for oxygen evolution reaction catalysis in wide pH solution, and origins of limited reconstruction degree as well as design strategies/principles toward complete reconstruction, 3) complete reconstruction for novel material synthesis and other electrocatalysis fields, and 4) advanced in situ/operando or multiangle/level characterization techniques to capture the dynamic reconstruction processes and real catalytic contributors. Finally, the existing major challenges and unexplored/unsolved issues on studying the reconstruction chemistry are summarized, and an outlook for the further development of complete reconstruction is briefly proposed. This review will arouse the attention on complete reconstruction materials and their applications in diverse fields.

This review article summarizes the recent advances in versatile synthesis strategies and broad applications of metal–organic framework coatings.

PKD2 and PKD1 genes are mutated in human autosomal dominant polycystic kidney disease. PKD2 can form either a homomeric cation channel or a heteromeric complex with the PKD1 receptor, presumed to respond to ligand(s) and/or mechanical stimuli. Here, we identify a two-residue hydrophobic gate in PKD2L1, and a single-residue hydrophobic gate in PKD2. We find that a PKD2 gain-of-function gate mutant effectively rescues PKD2 knockdown-induced phenotypes in embryonic zebrafish. The structure of a PKD2 activating mutant F604P by cryo-electron microscopy reveals a π- to α-helix transition within the pore-lining helix S6 that leads to repositioning of the gate residue and channel activation. Overall the results identify hydrophobic gates and a gating mechanism of PKD2 and PKD2L1.

Autosomal dominant polycystic kidney disease (ADPKD) is caused by mutations in PKD1 or PKD2 gene, encoding the polycystic kidney disease protein polycystin‐1 and the transient receptor potential channel polycystin‐2 (also known as TRPP2), respectively. Polycystin‐1 and polycystin‐2 form a receptor–ion channel complex located in primary cilia. The function of this complex, especially the role of polycystin‐1, is largely unknown due to the lack of a reliable functional assay. In this study, we dissect the role of polycystin‐1 by directly recording currents mediated by a gain‐of‐function (GOF) polycystin‐1/polycystin‐2 channel. Our data show that this channel has distinct properties from that of the homomeric polycystin‐2 channel. The polycystin‐1 subunit directly contributes to the channel pore, and its eleven transmembrane domains are sufficient for its channel function. We also show that the cleavage of polycystin‐1 at the N‐terminal G protein‐coupled receptor proteolysis site is not required for the activity of the GOF polycystin‐1/polycystin‐2 channel. These results demonstrate the ion channel function of polycystin‐1 in the polycystin‐1/polycystin‐2 complex, enriching our understanding of this channel and its role in ADPKD.

Transient receptor potential (TRP) channels are regulated by diverse stimuli comprising thermal, chemical, and mechanical modalities. They are also commonly regulated by phosphatidylinositol-4,5-bisphosphate (PIP2), with underlying mechanisms largely unknown. We here revealed an intramolecular interaction of the TRPP3 N and C termini (N-C) that is functionally essential. The interaction was mediated by aromatic Trp81 in pre-S1 domain and cationic Lys568 in TRP-like domain. Structure-function analyses revealed similar N-C interaction in TRPP2 as well as TRPM8/-V1/-C4 via highly conserved tryptophan and lysine/arginine residues. PIP2 bound to cationic residues in TRPP3, including K568, thereby disrupting the N-C interaction and negatively regulating TRPP3. PIP2 had similar negative effects on TRPP2. Interestingly, we found that PIP2 facilitates the N-C interaction in TRPM8/-V1, resulting in channel potentiation. The intramolecular N-C interaction might represent a shared mechanism underlying the gating and PIP2 regulation of TRP channels.

<p><strong>Abstract.</strong> Methane is a greenhouse gas emitted by a range of natural and anthropogenic sources. Atmospheric methane has been measured continuously from space since 2003, and new instruments are planned for launch in the near future that will greatly expand the capabilities of space-based observations. We review the value of current, future, and proposed satellite observations to better quantify and understand methane emissions through inverse analyses, down to the scale of point sources and in combination with suborbital (surface and aircraft) data. Current observations from GOSAT are of high quality but have sparse spatial coverage. They provide limited information to quantify methane emissions on a regional (100–1000 km) scale. TROPOMI to be launched in late 2016 is expected to quantify daily emissions on the regional scale and will also effectively detect large point sources. Future satellite instruments with much higher spatial resolution, such as the recently launched GHGSat with 50 × 50 m<sup>2</sup> resolution over targeted viewing domains, have the potential to detect a wide range of methane point sources. Geostationary observation of methane, still in the proposal stage, will have unique capability for mapping source regions with high resolution while also detecting transient "super-emitter" point sources. Exploiting the rapidly expanding satellite measurement capabilities to quantify methane emissions requires a parallel effort to construct high-quality spatially and sectorally resolved emission inventories. Partnership between top-down inverse analyses of atmospheric data and bottom-up construction of emission inventories is crucial to better understand methane emission processes and from there to inform climate policy.</p>

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Autosomal dominant polycystic kidney disease is caused by mutations in the membrane receptor PKD1 or the cation channel PKD2. TACAN (also termed TMEM120A), recently reported as an ion channel in neurons for mechanosensing and pain sensing, is also distributed in diverse non‐neuronal tissues, such as kidney, heart and intestine, suggesting its involvement in other functions. In this study, we found that TACAN is in a complex with PKD2 in native renal cell lines. Using the two‐electrode voltage clamp in Xenopus oocytes, we found that TACAN inhibits the channel activity of PKD2 gain‐of‐function mutant F604P. TACAN fragments containing the first and last transmembrane domains interacted with the PKD2 C‐ and N‐terminal fragments, respectively. The TACAN N‐terminus acted as a blocking peptide, and TACAN inhibited the function of PKD2 by the binding of PKD2 with TACAN. By patch clamping in mammalian cells, we found that TACAN inhibits both the single‐channel conductance and the open probability of PKD2 and mutant F604P. PKD2 co‐expressed with TACAN, but not PKD2 alone, exhibited pressure sensitivity. Furthermore, we found that TACAN aggravates PKD2‐dependent tail curvature and pronephric cysts in larval zebrafish. In summary, this study revealed that TACAN acts as a PKD2 inhibitor and mediates mechanosensitivity of the PKD2–TACAN channel complex. Key points TACAN inhibits the function of PKD2 in vitro and in vivo. TACAN N‐terminal S1‐containing fragment T160X interacts with the PKD2 C‐terminal fragment N580–L700, and its C‐terminal S6‐containing fragment L296–D343 interacts with the PKD2 N‐terminal A594X. TACAN inhibits the function of the PKD2 channel by physical interaction. The complex of PKD2 with TACAN, but not PKD2 alone, confers mechanosensitivity.