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Related Concept Videos

Assembly of Complex Microtubule Structures01:32

Assembly of Complex Microtubule Structures

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Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
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Mechanism of Lamellipodia Formation01:31

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Cells migrating in response to external stimuli form lamellipodia, which are thin membrane protrusions supported by a mesh of linked, branched, or unbranched actin filaments. These actin filaments interact with myosin motor proteins, creating the dynamic actomyosin complex within the cytoskeleton. Contractility, or the ability to generate contractile stress, is inherent to the actomyosin complex. It helps cells detect the stiffness of the surrounding ECM and exert contractile force for...
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Cytoskeletal Coordination in Cell Migration01:32

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A migrating cell changes its shape during the cyclic events of attachment and detachment from the substratum and repositions the cell organelles correspondingly. These complex events are orchestrated by the dynamic cytoskeletal network comprising actin filaments, intermediate filaments, and microtubules. Cytoskeletal crosstalk — the direct and indirect communication between the different components — is crucial for this coordination. Direct communication involves various linker...
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Protein Complex Assembly02:41

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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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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...
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The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
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Updated: Jun 13, 2025

Forming, Confining, and Observing Microtubule-Based Active Nematics
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Diverse Self-assembly Pathways in Nematic Compartment Network: Topological Percolation and Pathfinding.

Seongmin Jang1,2, Yong Woo Park1, Sunkuk Kim1

  • 1Department of Electrical and Computer Engineering, Sungkyunkwan University, Jangan-Gu, Suwon, Gyeonggi-do, 16419, Republic of Korea.

Small (Weinheim an Der Bergstrasse, Germany)
|September 17, 2024
PubMed
Summary

Confined nematic molecules in interconnected microcompartments create diverse patterns, unlike predictable single structures. Intercompartment communication drives this complexity, modeling controlled randomness for applications like anticounterfeit technology.

Keywords:
multiple assembly pathwaysnematic compartmentstopological defecttopological pathfindingtopological percolation

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Area of Science:

  • Soft Matter Physics
  • Materials Science
  • Network Science

Background:

  • Nematic molecule self-assembly in microcompartments typically yields predictable, single topological structures.
  • Surface anchoring conditions usually dictate predictable molecular organization.

Purpose of the Study:

  • To investigate molecular self-assembly in a confined nematic system with interconnected microcompartments.
  • To explore the emergence of diverse topological structures and patterns due to intercellular communication.

Main Methods:

  • Fabrication of an array of microcompartments linked by channels.
  • Observation and analysis of nematic molecular self-assembly within this interconnected system.
  • Modeling the domain structure using isotropically directed bond percolation.

Main Results:

  • Demonstrated diverse molecular assembly pathways leading to four topological structures and twelve random patterns.
  • Identified intercompartment communication via channels as critical for pattern diversity and domain formation.
  • Characterized domain structures exhibiting pathfinding and reverse tree properties.

Conclusions:

  • Interconnected microcompartments enable complex, multi-pattern nematic self-assembly, deviating from predictable single structures.
  • The system serves as a model for controlled randomness and restricted network growth.
  • Potential applications include anticounterfeit protection using physically unclonable functions (PUFs) with multi-level protocols.