Articles tagged with Kinesins
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Salk Institute and UC San Diego researchers captured the first-of-its-kind video of dynein-Lis1 protein interaction, revealing 16 detailed shapes that support designing therapeutics to restore dynein and Lis1 function. The insights gained from this movie will help identify precise locations where drugs can interact with the proteins.
A recent study has identified Kif23 as a key regulator of embryonic brain development, highlighting its potential link to microcephaly. The research found that Kif23 is essential for neural progenitor cell proliferation and differentiation, with deficiency leading to decreased cell growth and increased apoptosis.
A new study reveals that chloroplasts are essential for plant immunity, with stromules forming around the nucleus to transport pro-defense signals. Researchers have identified a key protein involved in stromule biogenesis during immunity, opening up new avenues for understanding and engineering resistance to pathogens.
Researchers from Tokyo University of Science reveal the crystal structure of centromere-associated protein E (CENP-E), a promising target for inhibitor therapy. The discovery is expected to facilitate the development of anticancer drugs with fewer adverse effects on patients.
Researchers at Okayama University discovered genes and proteins responsible for the rapid contraction of axopodia in Heliozoa, a group of eukaryotes. The study identified key players in microtubule disruption, including katanin p60, kinesin, and calcium signaling proteins.
Researchers discovered that Dis1 protein promotes microtubule shortening in fission yeast through catastrophe, a process where growing microtubules suddenly shorten. This finding challenges the conventional view of microtubule stabilization and has long-term applications for therapy and artificial cell segregation.
Researchers found that propofol decreases intracellular transport of proteins in neurons, impacting vesicle movement and axonal delivery. This study contributes to understanding how propofol causes anesthesia and may lead to the development of better anesthetic drugs.
A new study published in PLOS Biology reveals the significance of kinesins in basic cellular processes needed for malaria parasite development, multiplication and invasion. Researchers found that eight out of nine kinesins present in the parasite genome are required for cell proliferation to cell movement in mosquito hosts.
Researchers developed micro-sized machines utilizing swarming strategy for cargo delivery, outperforming single robots with efficiency of up to five times. The team created a swarm of cooperating robots that can divide workload and respond to risks, expanding potential uses for microrobots.
Researchers at Hokkaido University found that trimethylamine N-oxide (TMAO) can reversibly control the rigidity of kinesin-propelled microtubules, a crucial component of molecular machines. The study demonstrates a simple method to dynamically adjust MT property and functions.
A research team led by Associate Professor Akira Kakugo of Hokkaido University has provided direct evidence that microtubules function as mechanosensors, slowing down kinesin movement when bent. This phenomenon is attributed to enhanced interaction energy between kinesin and deformed microtubule structural units.
Scientists at UNIGE have developed a fluorescent dye to track the movement of kinesin proteins within cells, revealing their path and direction. This breakthrough enables researchers to study the fundamental question of protein transport and cargo distribution in cells.
Researchers at Rice University have discovered how propofol, a common anesthetic, disrupts the movement of kinesin proteins that deliver cargo along microtubules. The study found that propofol binding shortens the 'run length' of kinesin's motion by up to 60%, leading to its release from the microtubule and stopping its movement.
Researchers at the Centre for Genomic Regulation discovered that a type of kinesin called KIF3A/B transports mRNAs, enabling neurons to build their cellular skeleton and form new connections. This process is crucial for memory formation and storage, with mRNAs playing a key role in reinforcing synapses.
A Japanese research team has uncovered more about how proteins move using high-speed imaging to track dynein's movement along a microtubule. They found dynein moves erratically with frequent backward steps and side steps, challenging the conventional understanding of molecular motor tasks.
Researchers successfully used deep-sea osmolyte trimethylamine N-oxide (TMAO) to control biomolecular machines over a wide temperature range. TMAO suppresses thermal denaturation of kinesins in a concentration-dependent manner, allowing them to propel microtubules for a prolonged time.
Researchers discovered that two types of 'kinesin' molecular motors coordinate differently, with kinesin-1 working independently and kinesin-14 interacting to tune transport speed. This breakthrough expands understanding of cellular processes and basic life functions.
Researchers at Rensselaer Polytechnic Institute developed a novel imaging technique to visualize kinesin motor proteins and their cargo. The study shows that the 'smart motor' theory is not the only regulation at play, suggesting the involvement of adapter proteins.
Researchers at Hokkaido University developed a method to control swarming molecular machines using simple mechanical stimuli, exhibiting zigzag patterns or forming vortices. The system uses motor proteins and microtubules, which can self-repair after disruption.
Researchers at Hokkaido University successfully assembled a larger biomolecular motor system using DNA origami, overcoming previous scalability challenges. The system, combining fibrous microtubules and motor protein kinesins, exhibits dynamic contraction when energized by ATP.
Scientists developed a new microscopy technique to track protein molecular motors with atomic-level precision and microsecond time resolution. The system achieved 1.3 angstrom localization precision at 1 millisecond time resolution, revealing details of the kinesin motor's motion.
A team of researchers has used cryo-electron microscopy to study how microtubule-associated proteins regulate cell structure and transport. They found that MAP4 stabilizes microtubules while blocking kinesin's movement, which could lead to new treatment strategies for cardiac hypertrophy and neurodegenerative diseases.
Researchers found a key regulator, importin IMB4, that holds kinesins in check until their cargo is needed. This process is crucial for building the plant cell wall and preventing waste.
A microscopic 'railway' system in cells can adjust its structure to suit bodies' needs, with research suggesting stabilization by kinesin enzymes. This discovery could lead to improved treatments for diseases linked to microtubule abnormalities, such as Alzheimer's and cancer.
Researchers developed DNA-assisted molecular robots that autonomously swarm in response to chemical and physical signals. The swarm behavior resembles that of fish, ants, and birds, featuring complex structures, distinct divisions of labor, robustness, and flexibility.
A Rice University-led study shows that kinesins ignore weak forces as they transport cargo in cells, with lead kinesins carrying 90% of the load. The research provides molecular-level details of how kinesins respond to external forces and confirms earlier experiments on team-based motor proteins.
Scientists have developed a high-resolution microscope to directly observe kinesin motors moving along microtubules, revealing the coordination of attachment and release. This new understanding may help clarify defects in transport processes contributing to diseases such as Alzheimer's and ALS.
Researchers have identified a new adaptor protein on the microtubule roadway that helps motors navigate proteins to their correct destinations. This discovery challenges previous assumptions about motor function and has implications for understanding diseases such as cancer and cardiac disease.
Scientists employed kinesin motor proteins to detect stretching and compressing of soft silicon-based material polydimethylsiloxane (PDMS). The study found that microtubules moved faster and aligned themselves in response to stretching, while slowing down and aligning perpendicular to compression.
Researchers have discovered a new mutation that rescues abnormal axonal growth in the developing mouse brain affected by CFEOM3. The mutation targets the kinesin-microtubule interface and suppresses abnormal axon guidance.
Recent research by IPC PAS reveals how kinesin transports large molecules within cells, utilizing a unique 'silly walk' mechanism. By controlling the movement of kinesin, researchers confirmed one of earlier-known proposals of its mechanism.
A new study led by Columbia University researcher Henry Hess found that molecular shuttles degrade over time, similar to a car's wear and tear, when operating. The degradation is measured in terms of distance traveled, with equivalent wear occurring at just a millimeter for the shuttle.
Scientists have identified new therapeutic targets for memory disorders and developed a high-throughput screening test to uncover compounds that may treat these conditions. The study reveals the importance of kinesin proteins in regulating synaptic function and identifies potential drug candidates.
Scientists at Technical University of Munich created a simple cell model with a specific function using basic ingredients. The artificial cell can move and change shape without external influences, mimicking natural cell behavior.
Researchers at ETH Zurich have developed a nanoscale assembly line that uses mobile assembly carriers and biological motors to assemble complex substances. The system, which is three times thinner than a human hair, enables the selective modification of organic molecules and the assembly of nanotechnological components.
Researchers discovered that kinesin KIF13B concentrates at the cell membrane where LDL is taken up, and promotes endocytosis of LRP1 through caveolae. This unexpected role for a motor protein reveals a new mechanism for regulating blood cholesterol levels.
Researchers used laboratory experiments to test a model of microtubule steering, finding that kinesin motors can redirect microtubule ends into branches using crowd-sourced guidance from protein EB1. The study suggests this mechanism is a general strategy for organizing and maintaining proper microtubule polarity in cells.
Researchers at Rice University have found that motor proteins cooperate differently, with myosinVa producing more force than kinesin-1. This cooperation is crucial for regulating the transport of organelles within cells, and breakdowns in motor function are implicated in human diseases.
Scientists have developed a system that can construct its own network of tracks, transport cargo, and dismantle the tracks using DNA and nano-scale motors. The system is powered by ATP fuel and uses motor proteins to control the movement of cargo across the network.
Researchers discovered that a team of dynein motors can share a load much larger than any one motor can handle due to their ability to change gears. This allows them to work efficiently and generate large forces. In contrast, kinesin motors without gears cannot produce comparable forces.
Scientists have found that kinesins, molecular motors responsible for transporting proteins and chromosomes, exhibit spiral motion during transport. This finding challenges the long-held assumption of straight-line movement, suggesting a new perspective on their role in cell function.
Researchers found that molecular motor proteins fold in on themselves to prevent unnecessary energy consumption, controlling cargo transport. This discovery may open new avenues for treating neurodegenerative diseases such as Alzheimer's and Huntington's.
Researchers find that kinesins, powerful cargo-moving proteins, struggle to coordinate their efforts when paired, leading to inconsistent cargo transport. This discovery sheds light on the complex mechanisms governing intracellular transport and its link to neurodegenerative diseases.
Researchers at TUM and LMU investigate kinesin-2, a fast motor protein that transports cellular cargoes along microtubules. They find that KLP11 has an autoinhibition mechanism that allows it to control its speed and function in the cell.
A team of researchers has discovered that kinesin proteins use a string of water molecules to harness the energy of ATP breakdown. This breakthrough reveals a critical role for water molecules in cellular function and may lead to novel drugs to combat diseases. The study provides a clearer picture of how cells function and flourishes.
Researchers at Lawrence Berkeley National Laboratory have made the closest look yet at kinesin protein's structural changes as it ferries molecules within cells. The high-resolution snapshots show kinesin moving up and down like a seesaw, propelled by an energy-giving compound called ATP.
Researchers used laser tweezers to measure the friction between a single motor protein molecule and its track, showing that proteins work against resistance like macroscopic machines. The findings provide insight into the efficiency of kinesin motors and their role in cell division and muscle function.
Researchers have discovered that motor proteins can be engineered for efficient cargo transport, potentially leading to targeted cancer treatment. By altering the function of these proteins, scientists aim to develop new drugs that inhibit kinesin activity during cell division, slowing tumor growth.
A team of Dartmouth researchers has found a new function for the protein NOD, which plays a crucial role in chromosome segregation during cell division. This discovery contributes to our understanding of how cell functions can go wrong, particularly in cancerous cells.
Researchers at the University of Rochester have discovered that a previously unknown molecule controls the movement of organelles within cells. This finding has significant implications for understanding neurological diseases and developing new approaches to fighting pathogens.
MIT engineers have discovered that a specific region of the kinesin protein generates the force needed for its movement. The research, published in PNAS, sheds light on how this protein enables functions such as cell division and may one day aid in developing therapies for diseases like cancer.
A new study sheds light on how centromeric protein E (CENP-E) orchestrates chromosome movements at a critical stage of cell division. The researchers used a technique to watch CENP-E move along its microtubule tightrope, making key observations about its movement and force production.
A new study reveals a mechanism of regulating protein transport in neurons, where tau proteins act as smart speed bumps to regulate the movement of dynein and kinesin proteins. This finding provides insight into neurodegenerative diseases like Alzheimer's, which arise from impaired shipping systems.
A team of researchers at Weill Cornell Medical College discovered a molecular 'switch' that selects specific kinesin motor proteins to transport surface markers to their ultimate destinations on the cell's surface. This finding holds promise for developing targeted therapies with fewer side effects for diseases like cystic fibrosis and...
A team of researchers has captured images of molecular motors' structural changes using electron microscopy. The findings provide insights into the mechanisms behind these tiny molecules' movements, which power cellular processes like cell division.
Researchers at the University of Illinois Chicago discovered a molecular motor that helps cells determine which way is up by transporting a key lipid. This process is essential for maintaining cell polarity and preventing cancerous metastasis. The study sheds light on the trafficking and disposition of polarity determinants.
Researchers have developed a new classification system for myosins, increasing the number of subclasses from 18 to 24. This allows for better understanding of each myosin's function and its evolutionary links with other proteins.
Researchers have discovered that molecular motors dynein and kinesin do not compete for control when moving cellular cargo, but instead cooperate to produce more than 10 times the speed of individual motors. This cooperative behavior allows the cargo to move faster and with greater precision inside the cell.
Researchers discovered that kinesin molecules walk with a limp gait, taking asymmetric steps instead of regular strides. This finding has implications for understanding protein transport and potential therapies for diseases such as Huntington's and Alzheimer's.
Researchers used a two-dimensional optical force clamp to control and observe individual kinesin molecules, revealing that applying forces from the rear has no effect on its speed. This surprising finding challenges the existing hand-over-hand model of kinesin's movement.