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Bacteria form communities known as biofilms, which disassemble over time. In our studies outlined here, we found that, before biofilm disassembly, Bacillus subtilis produced a factor that prevented biofilm formation and could break down existing biofilms. The factor was shown to be a mixture of D-leucine, D-methionine, D-tyrosine, and D-tryptophan that could act at nanomolar concentrations. D-amino acid treatment caused the release of amyloid fibers that linked cells in the biofilm together. Mutants able to form biofilms in the presence of D-amino acids contained alterations in a protein (YqxM) required for the formation and anchoring of the fibers to the cell. D-amino acids also prevented biofilm formation by Staphylococcus aureus and Pseudomonas aeruginosa. D-amino acids are produced by many bacteria and, thus, may be a widespread signal for biofilm disassembly.

Inspect the file disassembly.txt and see what is located at address 0x014c2e. If it does not match what CCS shows, then something went wrong at some point after the program is built. An error may have happened when flashing or loading the program, or during program execution.

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Researchers at Oak Ridge National Laboratory developed a robotic disassembly system for used electric vehicle batteries to make the process safer, more efficient and less costly. Credit: Jenny Woodbery/ORNL, U.S. Dept. of Energy

With the anticipated growth in EVs over the next two decades comes the issue of how to recycle the large lithium-ion battery packs that power them. ORNL engineers put together a demonstration to show that robots can accelerate disassembly and make the process safer for workers while greatly increasing throughput.

Whether a recycler simply wants to get through the outer housing to access batteries and replace worn components, or completely recycle battery stacks for recovery of cobalt, lithium, metal foils and other materials, the first step is battery diagnostics for safe and efficient handling and disassembly.

Limiting human interaction is important for both safety and efficiency. The robots swiftly remove bolts and other housing regardless of any remaining charge, whereas human operators must undertake an exacting, lengthy process to discharge used batteries before breaking them down manually. Automated disassembly reduces human exposure to toxic chemicals found inside the batteries and high power levels that are approaching the 900-volt level in some newer vehicles.

The work builds on expertise developed in previous ORNL projects for the CMI that focused on robotic disassembly of hard drives for recovery of rare-earth magnets. Engineers also proved that those magnets can be directly reused in electric motors.

Cell Differentiation: Primary cilia are shown to be important for the maintenance and/or differentiation of stem cells such as mesenchymal stem cells, neural stem cells, etc. [63]. Interestingly, studies have shown that ciliary loss can occur when cells undergo differentiation both in mammalian cells and unicellular organisms. It is shown that when epithelial cells or mesenchymal fibroblasts differentiate to myofibroblast, cilia are completely disassembled and thereby significantly alter Hedgehog and platelet-derived growth factor (PDGF) signaling pathways that are known to regulate the cell differentiation process [64,65]. Ciliary loss has also been reported during different stages of protozoa, algae, and fungi [50]. In mammals, it is shown that delayed cilia disassembly can alter the fate of neural progenitor cells from self-renewal to premature differentiation and can cause microcephaly [66]. Given that cilia length has been positively correlated with activation of key signaling pathways (such as Sonic Hedgehog or PDGF) that are involved in stem cell differentiation, it will be interesting to evaluate the effect of changes in cilia disassembly rate on the lineage commitment or differentiation of various stem cells.

Among the different regulatory players, calcium (Ca2+) and calmodulin (CaM) are important for forming the HEF1-AurA complex and activating AurA kinase at the basal body during the ciliary disassembly process [40,79]. PDGFR has also been shown to promote cilium disassembly by activating phosphoinositide phospholipase C gamma, which causes the release of intracellular Ca2+ and activation of CaM and AurA [80]. Collectively, these data show that signaling pathways that cause the release of intracellular Ca2+ and activation of CaM could indirectly lead to AurA activation and thereby promote ciliary disassembly.

Transcriptional regulation of AurA is also shown to be important in regulating the process of ciliary disassembly, apart from its direct activation or stabilization, as discussed above. Studies show that inositol polyphosphate-5-phosphatase E (INPP5E) regulates AurA protein levels by increasing AurA transcript levels by AKT activation, which can impact the ciliary disassembly process [87]. Fibroblast growth factor receptor 1 oncogene partner is also shown to affect cilia disassembly by regulating AurA expression [88]. AurA transcription is also shown to be regulated by different signaling pathways, including, ERK-responsive Ets pathway, STAT5, estrogen/GATA3, HIF1, etc. [89]. As the majority of these studies were performed in cancer cells, the transcriptional regulation of AurA was mainly associated with its role in mitosis and cell proliferation. However, whether these signaling pathways affect cilia disassembly by regulating AurA and its implications on cancer cells in the G0/G1/S phase of the cell cycle is largely unexplored.

Besides direct activation, stabilization, or transcriptional regulation of ciliary disassembly factors, cellular localization can also impact the cilia disassembly process. It is shown that SH2-containing phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase implicated in phosphoinositide signaling can relocate AurA and HEF1 from the apical to the basolateral surface of epithelial cells and thereby promote cilia formation in epithelial cells toward tubular lumen [90]. Proteins that aid in the stabilization or activation of AurA also gets localized near the basal body. Pitchfork (PIFO) is known to be localized at the basal body and can activate AurA during the process of ciliary disassembly [91]. Interestingly, it is suggested that AurA belongs to a primary cilium disassembly complex (CDC) containing CPAP, NDE1, and OFD1 [66]. This complex, upon mitogenic signaling, assembles near the basal body and aid in the process of cilia disassembly. Further studies are required to evaluate if cilia disassembly associated proteins such as PIFO, PCM1, or PLK1 are a part of or transiently interact with the CDC complex during the ciliary disassembly process.

The base of the cilium is surrounded by the ciliary pocket, a structure rich in actin network density. Remodeling of the ciliary pocket membrane during disassembly is mediated by TCTEX-1 (DYNLT1, dynein light chain-1), which is activated by phosphorylation at T94. TCTEX-1 was initially described as a light chain subunit of cytoplasmic dynein [104], and the role of phosphorylated T94 TCTEX-1 in regulating cilia disassembly has been described in cortical neuronal progenitors cells [105]. Phosphorylation of TCTEX-1 at T94 is required for both cilium resorption and entry into the S phase of the cell cycle. Mechanistically, phosphorylation of TCTEX-1 at T94 leads to the dissociation of TCTEX-1 from the dynein complex, facilitating cilia resorption. TCTEX-1 activates F-actin polymerization triggering a cascade of events that coordinately lead to cilia resorption and cytoskeletal rearrangement [105]. The active form of TCTEX-1 binds to annexin A2, actin-related protein 2/3 complex subunit 2, and cell division control protein 42, which actively regulates actin dynamics and clathrin-dependent endocytosis at the ciliary base, thus mediating the remodeling of the ciliary pocket membrane during cilia disassembly [106]. Inhibition of phosphorylation of TCTEX-1 at T94 induces neuronal differentiation instead of proliferation, highlighting its importance in coupling ciliary disassembly and cell cycle progression. More recently, it has also been shown that exocysts localized near the ciliary base assist in recycling the resorbed cilia and en route the ciliary components back to the cell surface. Whether and how this process affects ciliary disassembly is a subject of further investigation [107].

From a technical standpoint, since cellular processes such as cell cycle and differentiation are tightly coupled with cilia dynamics, many proteins that regulate these processes are found to affect ciliary length. In addition, certain proteins might play a role in both cilia assembly and disassembly, possibly via different mechanisms. Hence, in order to tease out the role of such proteins in cilia dynamics, future studies may require the use of more refined techniques such as auxin-inducible degron-mediated protein degradation and use of proteolysis-targeting chimera to temporarily and spatially knockdown protein levels, especially during cilia disassembly. Additionally, tracking the cilia disassembly of single cells with confocal and time-lapse microscopy will also help decipher the mechanisms and sequence of events during cilia disassembly.

The primary cilium is an antenna-like, immotile organelle present on most types of mammalian cells, which interprets extracellular signals that regulate growth and development. Although once considered a vestigial organelle, the primary cilium is now the focus of considerable interest. We now know that ciliary defects lead to a panoply of human diseases, termed ciliopathies, and the loss of this organelle may be an early signature event during oncogenic transformation. Ciliopathies include numerous seemingly unrelated developmental syndromes, with involvement of the retina, kidney, liver, pancreas, skeletal system and brain. Recent studies have begun to clarify the key mechanisms that link cilium assembly and disassembly to the cell cycle, and suggest new possibilities for therapeutic intervention. 2351a5e196