AI Article Synopsis
- Nucleation has been the main focus of microtubule generation studies, but severing is highlighted as an alternative mechanism that creates new polymer ends in response to light in plants.
- CLASP is identified as a key protein that stabilizes new plus ends formed by severing, which is crucial for the correct reorientation of microtubule arrays in plant cells.
- Mutants lacking CLASP show impaired stabilization of these ends and reduced microtubule amplification, revealing the importance of CLASP in this process through computational modeling.
Article Abstract
Central to the building and reorganizing cytoskeletal arrays is creation of new polymers. Although nucleation has been the major focus of study for microtubule generation, severing has been proposed as an alternative mechanism to create new polymers, a mechanism recently shown to drive the reorientation of cortical arrays of higher plants in response to blue light perception. Severing produces new plus ends behind the stabilizing GTP-cap. An important and unanswered question is how these ends are stabilized in vivo to promote net microtubule generation. Here we identify the conserved protein CLASP as a potent stabilizer of new plus ends created by katanin severing in plant cells. mutants are defective in cortical array reorientation. In these mutants, both rescue of shrinking plus ends and the stabilization of plus ends immediately after severing are reduced. Computational modeling reveals that it is the specific stabilization of severed ends that best explains CLASP's function in promoting microtubule amplification by severing and array reorientation.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6314540 | PMC |
| http://dx.doi.org/10.1083/jcb.201805047 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Block Copolymer Electrolytes with Double Primitive Cubic Structures: Enhancing Solid-State Lithium Conduction via Lithium Salt Localization.
ACS Nano
January 2025
Department of Chemistry, Pohang University of Science and Technology (POSTECH), Pohang 37673, Republic of Korea.
We present a strategy for enhancing Li conduction in block copolymer electrolytes by introducing trace amounts of Li salts into polystyrene--poly(ethylene oxide) (PS--PEO), wherein Li ions preferentially coordinate with the -OH end groups of the PEO chains, resulting in the formation of double primitive cubic (3̅) structures. Compared with TFSI anions in Li salts, smaller anions (PF and BF) could facilitate ion localization more effectively, expanding the salt concentration range for developing stable 3̅ structures. The 3̅ structures formed in PS--PEOs doped with LiBF at = 0.
View Article and Find Full Text PDFMolecular features and expression kinetics of interleukin-10 gene from the marine teleost, Snubnose pompano (Trachinotus blochii).
Mol Biol Rep
December 2024
Marine Biotechnology, Fish Health, and Nutrition Division, ICAR-Central Marine Fisheries Research Institute, Post Box No. 1603, Ernakulam North P.O, Kochi, 682 018, India.
Background: Interleukin 10 (IL-10) is uniquely positioned in the immune regulation of teleosts. Modifying the IL-10 pathway changes the teleost's disease susceptibility; however, there is no data on its post-transcriptional regulation. Trachinotus blochii is a high-value mariculture species.
View Article and Find Full Text PDFBending stiffness of Toxoplasma gondii actin filaments.
J Biol Chem
December 2024
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520. Electronic address:
Article Synopsis
- Actin is crucial for the Apicomplexan parasite Toxoplasma gondii, supporting key processes like invasion and organelle inheritance, and its unique properties enable rapid treadmilling compared to vertebrate actin.
- Recent findings suggest that although T. gondii actin (TgAct1) has weaker interactions at its D-loop, this does not significantly impair its bending stiffness or stability, making it similar to vertebrate actin.
- Structural analysis shows that despite the differences at the D-loop, TgAct1 filaments maintain stabilizing features, indicating a mechanism where weak D-loop interactions affect subunit addition at the ends but not within the filament itself.
End Binding Proteins: Drivers of Cancer Progression.
Cytoskeleton (Hoboken)
December 2024
Department of Biotechnology, University of Kerala, Kariavattom Campus, Thiruvananthapuram, India.
Cancer, a complex and heterogeneous disease, continues to be a major global health concern. Despite advancements in diagnostics and therapeutics, the aggressive nature of certain cancers remain a significant challenge, necessitating a deeper understanding of the underlying molecular mechanisms driving their severity and progression. Cancer severity and progression depend on cellular properties such as cell migration, cell division, cell shape changes, and intracellular transport, all of which are driven by dynamic cellular microtubules.
View Article and Find Full Text PDFMyosin-dependent short actin filaments contribute to peripheral widening in developing stereocilia.
Res Sq
December 2024
Department of Biology, Indiana University, Indianapolis, IN.
Article Synopsis
- In the auditory and vestibular systems, stereocilia are specialized structures that convert sound and motion into electrical signals, with their growth involving the addition of actin filaments.
- Research focused on how stereocilia widen during development, finding that new actin filaments first incorporate at the tips before spreading along the shaft, indicating that the core structure remains stable.
- The study revealed a previously unrecognized population of short actin filaments at the tips of stereocilia, which are influenced by specific myosin motors (MYO3A/B and MYO15A) that play a crucial role in their growth and stabilization, suggesting these interactions are important for proper mechanosensory function.
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!