The Game of Tubulins
1Molecular Pathology, Department of Translational Medicine, Lund University, Skåne University Hospital, 20502 Malmö, Sweden.
Cells
|April 3, 2021
Summary
Tubulin superfamily members are essential GTPases regulating cell structure and function. This review compares GTP-binding domains of alpha, beta, and gamma-tubulin, highlighting gamma-tubulin
Area of Science:
- Biochemistry
- Cell Biology
- Molecular Biology
Background:
- Tubulin superfamily proteins are essential GTPases vital for cellular functions.
- They form microtubules and the gamma-tubulin meshwork, crucial for cell structure.
- Dysregulation of tubulin is implicated in developmental brain disorders and cancer.
Purpose of the Study:
- To compare the GTP-binding domains of alpha-tubulin, beta-tubulin, and gamma-tubulin.
- To elucidate the role of the gamma-tubulin GTP-binding domain in regulating the gamma-tubulin meshwork.
- To understand the impact of gamma-tubulin on cellular homeostasis.
Main Methods:
- Comparative analysis of GTP-binding domain structures and sequences.
- Review of existing literature on tubulin function and regulation.
- Functional implications of structural similarities and differences.
Main Results:
- Identified conserved and divergent features within the GTP-binding domains of alpha, beta, and gamma-tubulin.
- Highlighted the critical role of the gamma-tubulin GTP-binding domain in meshwork organization.
- Established links between GTP-binding domain activity and cellular homeostasis.
Conclusions:
- The GTP-binding domain is fundamental to tubulin function across the superfamily.
- Gamma-tubulin's GTP-binding domain plays a unique and vital role in cellular organization and stability.
- Understanding these domains offers therapeutic targets for brain disorders and cancer.
Related Concept Videos
Microtubule Instability
5.5K
Microtubules are hollow cylindrical filaments having a diameter of approximately 25 nm and a length that varies from 200 nm to 25 μm. GTP-bound tubulin subunits form αβ-heterodimers for microtubule assembly. These core building blocks interact longitudinally, polymerizing into protofilaments. The protofilaments then interact with one another through lateral bonding forces to form stable cylindrical microtubules. These cylindrical filaments are dynamic as they undergo repeated...
5.5K
Microtubules
9.0K
Microtubules are the thickest cytoskeletal filaments with a diameter of 25 nm. In prokaryotic organisms, microtubules are commonly found in locomotory appendages like cilia and flagella. In eukaryotic cells, microtubules form specialized extensions for moving fluid over the surface, like those found in cells lining the intestine.
Microtubules have two structurally similar globular protein subunits: α and β tubulins. In the cytosol, the α and β tubulins form a heterodimer....
Microtubules have two structurally similar globular protein subunits: α and β tubulins. In the cytosol, the α and β tubulins form a heterodimer....
9.0K
Microtubules
95.8K
There are three types of cytoskeletal structures in eukaryotic cells—microfilaments, intermediate filaments, and microtubules. With a diameter of about 25 nm, microtubules are the thickest of these fibers. Microtubules carry out a variety of functions that include cell structure and support, transport of organelles, cell motility (movement), and the separation of chromosomes during cell division.
95.8K
Assembly of Cytoskeletal Filaments
24.8K
Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
24.8K
Actin Treadmilling
8.9K
Actin filaments undergo polymerization and depolymerization from either end. The polymerization and depolymerization rates depend on the cytosolic concentration of free G-actins. The polymerization rate is generally higher at the plus or barbed end, while the depolymerization rate is higher at the minus or pointed end. At a steady state, critical concentration describes the concentration of free G-actin monomers at which the polymerization rate at the plus end is equal to that of the...
8.9K
Cytoskeletal Proteins in Bacteria
3.8K
Bacterial cells were initially considered simple, randomly organized structures lacking a cytoskeleton. However, the discovery of cytoskeleton homologs in bacteria led to the change of this opinion. Bacterial cytoskeletal filaments regulate the cell shape, cell polarity, cell division, and partitioning of plasmids during cell division. It was later discovered that bacterial cytoskeletal proteins, mainly actin and tubulin homologs, are diverse compared to their eukaryotic counterparts. On the...
3.8K


