Using double-label immunofluorescence and electron microscopy we studied the interaction between microtubules (MT) and intermediate filaments (IF) in MO cells treated with various combinations of taxol and nocodazole. With taxol, the organized MT of cultured cells are replaced by free MT and MT bundles. This rearrangement of MT is followed by a rearrangement of the IF. As in untreated cells a close association between these two filamentous systems is observed. In cells pretreated with nocodazole followed by addition of taxol, to induce the bundles of free MT, the preexisting IF coils disappear and IF associate with the MT. From these experiments we conclude that an interaction between MT and IF exists independent of the normal organisation of the MT system. The redistribution of IF always follows the redistribution of MT. The data show that MT determine the spatial distribution of IF which most probably involves some kind of physicochemical link.
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http://dx.doi.org/10.1016/0309-1651(83)90103-0 | DOI Listing |
Nat Mater
January 2025
Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA, USA.
Cells use 'active' energy-consuming motor and filament protein networks to control micrometre-scale transport and fluid flows. Biological active materials could be used in dynamically programmable devices that achieve spatial and temporal resolution that exceeds current microfluidic technologies. However, reconstituted motor-microtubule systems generate chaotic flows and cannot be directly harnessed for engineering applications.
View Article and Find Full Text PDFFEBS J
January 2025
Central European Institute of Technology, Masaryk University, Brno, Czech Republic.
Microtubule associated protein 2 (MAP2) interacts with the regulatory protein 14-3-3ζ in a cAMP-dependent protein kinase (PKA) phosphorylation dependent manner. Using selective phosphorylation, calorimetry, nuclear magnetic resonance, chemical crosslinking, and X-ray crystallography, we characterized interactions of 14-3-3ζ with various binding regions of MAP2c. Although PKA phosphorylation increases the affinity of MAP2c for 14-3-3ζ in the proline rich region and C-terminal domain, unphosphorylated MAP2c also binds the dimeric 14-3-3ζ via its microtubule binding domain and variable central domain.
View Article and Find Full Text PDFWorld J Gastrointest Surg
January 2025
Department of Colorectal Surgery, The First Affiliated Hospital of Zhejiang Chinese Medical University (Zhejiang Provincial Hospital of Traditional Chinese Medicine), Hangzhou 310006, Zhejiang Province, China.
Background: Unraveling the pathogenesis of colorectal cancer (CRC) can aid in developing prevention and treatment strategies. Aurora kinase A (AURKA) is a key participant in mitotic control and interacts with its co-activator, the targeting protein for Xklp2 (TPX2) microtubule nucleation factor. AURKA is associated with poor clinical outcomes and high risks of CRC recurrence.
View Article and Find Full Text PDFPNAS Nexus
January 2025
Department of Biochemistry, University of Geneva, 1211 Geneva, Switzerland.
The microtubule cytoskeleton is a dynamic network essential for many cellular processes, influenced by physicochemical factor, such as temperature, pH, dimer concentration, and ionic environment. In this study, we used in vitro reconstitution assays to examine the effects of four monovalent ions (Na, K, Cl, and Ac) on microtubule dynamics, uncovering distinct effects for each ion. Na was found to increase microtubule dynamicity by raising catastrophe frequency, polymerization and depolymerization speeds, and ultimately reducing microtubule lifetime by 80%.
View Article and Find Full Text PDFJ Chem Inf Model
January 2025
Department of Chemistry, Faculty of Science, University of Waterloo, Waterloo, Ontario N2L 3G1, Canada.
Tau is a microtubule (MT)-associated protein that binds to and stabilizes the MTs of neurons. Due to its intrinsically disordered nature, it undergoes several post-translational modifications (PTMs) that are intricately linked to both the physiological and pathophysiological roles of Tau. Prior research has shown phosphorylation and O-GlcNAcylation to have contrasting effects on Tau aggregation; however, the precise molecular mechanisms and potential synergistic effects of these modifications remain elusive.
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