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Related Concept Videos

Laminins are the Adhesive Proteins of Basal Lamina00:55

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Laminins are heterotrimeric proteins with high molecular mass found in the extracellular matrix. Each laminin molecule is composed of three chains, viz. alpha, beta, and gamma, coded by five, four, and three paralogous genes, respectively. Laminins are categories based on the compositions of the three chains.
In humans, the five forms of alpha chains are LAMA 1, LAMA 2, LAMA 3, LAMA 4, and LAMA 5. The four forms of beta chains are LAMB 1, LAMB 2, LAMB 3, and LAMB 4. The three forms of gamma...
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Type IV collagen is a 400 nm long, network-forming collagen that acts as a barrier between the epithelial and endothelial cells. Type IV collagen  forms the backbone of the basement membrane by scaffolding with laminin, entactin, proteoglycans, and fibronectin. Apart from rendering structural support to the basement membrane, it also helps entail signaling potentials necessary for both pathological and physiological functions.
A type IV collagen molecule has six alpha chains which can...
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Types of Intermediate Filaments01:31

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The intermediate filaments are an essential component of the cytoskeleton. Presently six types of intermediate filament have been identified. Type I and II are acidic and basic keratin proteins. Type III is of mesodermal origin and comprises four proteins: vimentin, desmin, glial fibrillary acidic protein (GFAP), and peripherin. Vimentin is commonly found in mesenchymal cells, desmin in muscle cells, GFAP in astrocytes, while peripherin is found in peripheral nervous system neurons (PNS). Type...
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Disassembly of Intermediate Filaments01:35

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Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
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Formation of Intermediate Filaments00:57

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Intermediate filaments are cytoskeletal proteins with higher tensile strength and flexibility than microfilaments and microtubules. Unlike the other two cytoskeletal proteins, intermediate filament formation lacks the enzymatic activity to hydrolyze nucleotides like ATP and GTP to generate energy for polymerization. Therefore, the formation of intermediate filaments is multistep self-assembly. The involvement of any accessory proteins in intermediate filament formation has not yet been...
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Formation of Higher-order Actin Filaments01:11

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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.
The high-order actin...
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Generating a Fractal Microstructure of Laminin-111 to Signal to Cells
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Lateral A11 type tetramerization in lamins.

Anastasia V Lilina1, Anastasia A Chernyatina1, Dmytro Guzenko1

  • 1Laboratory for Biocrystallography, Department of Pharmaceutical and Pharmacological Sciences, KU Leuven, Belgium.

Journal of Structural Biology
|October 15, 2019
PubMed
Summary
This summary is machine-generated.

The A11 interaction in nuclear lamins (IFs) involves antiparallel tetramerization of coiled-coil dimers. This study reveals the molecular basis of this interaction, crucial for understanding intermediate filament assembly and related diseases.

Keywords:
Coiled coilIntermediate filamentsNuclear laminsX-ray crystallography

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Area of Science:

  • Structural biology
  • Biochemistry
  • Cell biology

Background:

  • Intermediate filaments (IFs), including nuclear lamins, assemble via lateral and longitudinal interactions of coiled-coil dimers.
  • The A11 assembly mode relies on antiparallel tetramerization of the coil1b segment.
  • Previous cryo-EM studies suggested lamin filaments are formed by two antiparallel dimer threads, but molecular details were lacking.

Purpose of the Study:

  • To elucidate the molecular basis of the A11 interaction in nuclear lamins.
  • To provide high-resolution structural insights into lamin filament assembly.

Main Methods:

  • X-ray crystallography of a lamin A fragment (residues 65-222) at 2.6 Å resolution.
  • Structural analysis of the coiled-coil interactions and lamin-specific inserts.

Main Results:

  • The crystal structure reveals the molecular details of the A11 interaction, confirming antiparallel tetramerization.
  • A continuous α-helical structure was observed in the preceding linker L1 region.
  • Unique interactions within the lamin-specific 42-residue insert in coil1b were identified, maintaining common structural principles with other IFs.
  • The A11 interaction in lamins appears weaker than in cytoplasmic IFs, despite a longer overlap.

Conclusions:

  • The study establishes the structural basis of the A11 interaction in nuclear lamins.
  • Understanding these interactions is fundamental for comprehending IF assembly mechanisms.
  • This knowledge is essential for investigating the molecular basis of diseases linked to IF mutations.