Collisions of Cortical Microtubules with Membrane Associated Myosin VIII Tail

Sefi Bar-Sinai1, Eduard Belausov1, Vikas Dwivedi1

  • 1The Institute of Plant Sciences, Volcani Institute, ARO, Rishon LeZion 7528809, Israel.

Cells
|January 11, 2022
PubMed

Insights

Myosin VIII ATM1 tail, a plasma membrane protein, influences cortical microtubule (MT) organization. Collisions between MTs and ATM1 tail clusters alter MT dynamics, contributing to their coordinated arrangement.

Area of Science:

  • Plant Cell Biology
  • Cytoskeletal Dynamics
  • Plasma Membrane Proteins

Background:

  • Cortical microtubules (MTs) and plasma membrane proteins often exhibit coordinated distribution.
  • The prevailing hypothesis suggests MTs inhibit protein diffusion, organizing membrane proteins.
  • The stability of myosin VIII ATM1 tail's membrane position prompted investigation into its role in MT organization.

Purpose of the Study:

  • To investigate the reciprocal relationship between myosin VIII ATM1 tail and cortical microtubule organization.
  • To determine if myosin VIII ATM1 tail influences microtubule organization due to its stable membrane localization.

Main Methods:

  • Co-localization studies of myosin VIII ATM1 tail and remorin 6.6.
  • Observation of microtubule (MT) dynamics upon overexpression of myosin VIII ATM1 tail.
  • Analysis of collisions between MTs (labeled with EB1) and ATM1 tail clusters.

Main Results:

  • Myosin VIII ATM1 tail co-localized with remorin 6.6, another stable membrane protein.
  • Overexpression of myosin VIII ATM1 tail resulted in reduced MT orientation dispersion.
  • Collisions between MTs and ATM1 tail clusters led to varied outcomes, including altered elongation rates and direction changes.
  • MT tracks (EB1) exhibited increased straightness in the presence of ATM1 tail.

Conclusions:

  • Myosin VIII ATM1 tail's stable membrane association can influence cortical MT organization.
  • Collisions between MTs and ATM1 tail-labeled structures contribute to the coordinated organization of MTs.
  • This study reveals a potential mechanism where membrane proteins actively shape cytoskeletal organization.

Related Concept Videos

Cell Motility through Blebbing01:16

Cell Motility through Blebbing

Blebs are a type of membrane protrusion formed by the internal hydrostatic pressure of the cytoplasm. Blebs are observed in several cell types, including fibroblasts, immune cells, and single-celled organisms like the amoeba. The primary function of blebs is cell locomotion and apoptosis, but they are also found during necrosis and cell division. The life cycle of a bleb comprises an initiation phase followed by the expansion and retraction phases.
Blebbing Through the Matrix
In multicellular...
2.1K
Microtubule Instability02:17

Microtubule Instability

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...
5.3K
Microtubule Associated Motor Proteins01:32

Microtubule Associated Motor Proteins

Eukaryotic cells have different motor proteins for transporting various cargo within the cell. These motor proteins differ based on the filament they associate with, the direction they move within the cell, and the type of cargo they transport. Motor proteins that associate with microtubules are known as microtubule-associated motor proteins. There are two families of microtubule-associated motor proteins —Kinesins and Dyneins. Both these proteins assist in the transport of cellular...
8.6K
Role of Myosin in Cell Migration01:18

Role of Myosin in Cell Migration

Myosins are multimeric motor proteins involved in various cellular processes such as migration, adhesion, and proliferation. Myosin II is the most common type in animal cells, which binds and cross-links actin filaments.
Myosin II  is a hexamer comprising two heavy chains with globular heads and coiled-coil tails, two regulatory light chains, and two essential light chains. The ATPase sites on the myosin heads hydrolyze ATP, and the released phosphate generates the force for contraction....
2.5K
Overview of Myosin Structure and Function01:15

Overview of Myosin Structure and Function

Myosins are a family of molecular motor proteins, first identified in the skeletal muscles, where they are responsible for muscle contraction. Along with their role in muscle contraction, these proteins also play a role in the intracellular transport of molecules and vesicles. There are twenty-four classes of myosins based on their domain sequence and organization. Of the twenty-four, six classes (Myosin I, Myosin II, Myosin V, Myosin VI, Myosin VII, and Myosin X)  have been well...
5.0K
The Movement of Organelles and Vesicles01:43

The Movement of Organelles and Vesicles

In eukaryotic cells,  cytoskeletal filaments such as actin, microtubules, and intermediate filaments form a mesh-like cytoskeletal network. These filaments serve as tracks for transporting cellular cargo. Specialized motor proteins use the chemical energy stored in adenosine triphosphate (ATP) for this transport. During interphase, microtubules are polarized, with the plus-end towards the cell periphery and the minus-end towards the cell center. Two microtubule-associated motor proteins,...
4.8K