Tubulin-like Proteins
Tubulin-like Proteins - Related Videos
02:40
Second Harmonic Generation Imaging in a Rat Model to Study Tubulin Defects
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2025
Source: Piazza, V., et al., Label-Free Non-Linear Optics for the Study of Tubulin-Dependent Defects in Central Myelin. J. Vis. Exp. (2023)This video demonstrates the procedure for imaging microtubule abnormalities in a rat brain tissue slice using a two-photon excitation microscope. It employs second harmonic generation (SHG) signals to detect tubulin defects and reduced myelin production.
02:04
Protein-protein Interfaces
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2020
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
06:30
Optimizing Tubulin Yield from Porcine Brain Tissue
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2024
This protocol describes a technique for the high-yield isolation of tubulin from the porcine brain optimized for small-scale instrumentation. The isolation procedures are complemented by procedures for determining tubulin polymerization activity in vitro using co-sedimentation assays and transmission electron microscopy.
08:07
Label-Free Non-Linear Optics for the Study of Tubulin-Dependent Defects in Central Myelin
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2023
In this article, we present a protocol to detect microtubule-loaded oligodendrocytes in a model of tubulinopathy through a simple, innovative second harmonic generation microscopy approach.
08:46
Green Fluorescent Protein-based Expression Screening of Membrane Proteins in Escherichia coli
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Cited by 34 •
2015
A streamlined approach to screening for the expression of recombinant membrane proteins in Escherichia coli based on fusion to green fluorescent protein is presented.
FAQs
A tubulin-like protein’s nucleotide state helps determine whether its filament is favored to grow or disassemble. GTP binding supports the assembly cycle, while GTP hydrolysis provides a chemical transition that can alter filament behavior; associated proteins further regulate these dynamics. This coupling allows cytoskeletal structures to remain responsive rather than fixed, which is important for changing cellular organization.
Their common features do not imply identical cellular roles. Eukaryotic tubulin is associated with microtubules, whereas bacterial FtsZ organizes a division ring. Other members participate in cell shape, intracellular organization, or chromosome segregation. Thus, related structural and nucleotide-dependent behavior can be adapted to different cellular tasks across organisms.
Associated proteins help regulate how filaments grow and disassemble, complementing control from the nucleotide state. This regulation can tune the timing and extent of cytoskeletal rearrangements. Because different tubulin-like proteins operate in distinct cellular settings, associated proteins provide a way to adapt a shared assembly mechanism to specialized functions.
FtsZ contributes to bacterial cell division by assembling into a ring whose filament system is governed by the same broad nucleotide-dependent dynamics described for tubulin-related proteins. The ring supplies an organized cytoskeletal structure at the division site. This example connects GTP-regulated filament behavior with a specific cellular event rather than with general intracellular organization alone.
Their value as antimicrobial targets comes from the connection between bacterial cytoskeletal dynamics and cell division. FtsZ is especially relevant because it forms the division ring, making its assembly behavior a useful focus for investigating how bacterial proliferation might be disrupted. The topic therefore links basic filament biology with research on strategies directed at microbial cells.
Comparing their structures, nucleotide-linked assembly, and cellular roles can clarify how cytoskeletal systems evolved. The comparison spans eukaryotic microtubules, bacterial division rings, and other functions such as cell shape, intracellular organization, and chromosome segregation. These relationships also help explain the molecular basis of cytoskeletal dynamics across biologically distinct systems.