Emerging Insights into the Function of Kinesin-8 Proteins in Microtubule Length Regulation

Sanjay Shrestha1, Mark Hazelbaker2, Amber L Yount3

  • 1Medical Sciences Program, Indiana University, Bloomington, IN 47405, USA. sashrest@indiana.edu.

Biomolecules
|December 23, 2018
PubMed

Insights

Kinesin-8 motor proteins regulate microtubule (MT) dynamics crucial for cell division. This review highlights recent findings on Kinesin-8 structure, function, and the role of its C-terminal tail in controlling MT length.

Area of Science:

  • Cell Biology
  • Molecular Motors
  • Mitosis

Background:

  • Microtubule (MT) dynamics are essential for cell division processes like spindle assembly and chromosome segregation.
  • Numerous cellular factors regulate MT dynamics, with Kinesin-8 family motor proteins playing a key role.
  • Kinesin-8 proteins function as MT-destabilizing factors, controlling MT length in a precise manner.

Purpose of the Study:

  • To review recent advancements in understanding the structure and function of the Kinesin-8 motor domain.
  • To explore the role of the Kinesin-8 C-terminal tail in regulating motor activity and localization.

Main Methods:

  • Literature review of recent research on Kinesin-8 motor proteins.
  • Analysis of structural and functional data related to Kinesin-8 domains.
  • Synthesis of findings on C-terminal tail contributions.

Main Results:

  • Detailed insights into the structure and catalytic mechanisms of the Kinesin-8 motor domain.
  • Evidence for the C-terminal tail's involvement in modulating Kinesin-8 motor activity.
  • Understanding of how the C-terminal tail influences Kinesin-8 protein localization within the cell.

Conclusions:

  • Kinesin-8 motor proteins are critical regulators of microtubule dynamics during mitosis.
  • Both the motor domain and the C-terminal tail are integral to Kinesin-8 function and localization.
  • Further research into Kinesin-8 regulation can provide insights into cell division control.

Related Concept Videos

Microtubules01:35

Microtubules

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.
99.1K
Regulated Protein Degradation02:58

Regulated Protein Degradation

It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
8.9K
Regulated Protein Degradation02:58

Regulated Protein Degradation

3.2K
Structural Protein Function01:56

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to...
29.9K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
9.6K
Protein-protein Interfaces02:04

Protein-protein Interfaces

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...
14.7K