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Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
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The adherens junctions that anchor cells together are multi-protein complexes that dynamically adapt to mechanical stimuli such as tensile forces and shear stress. Mechanosensory proteins in these junctions can sense such mechanical stimuli and undergo a shift in their conformation, resulting in an altered function — a process called mechanotransduction.
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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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The ciliary structures were first seen in 1647 by Antonie Leeuwenhoek while observing the protozoans. In lower organisms, these appendages are responsible for cell movement, while in higher organisms, these appendages help in the movement of the extracellular fluids within the body cavities.
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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,...
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Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro
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Dynamin Functions and Ligands: Classical Mechanisms Behind.

Mahaveer Singh1, Hemant R Jadhav2, Tanya Bhatt2

  • 1Department of Pharmacy, Birla Institute of Technology and Sciences Pilani, Pilani Campus, Rajasthan, India mahaveer2singh@gmail.com.

Molecular Pharmacology
|November 24, 2016
PubMed
Summary
This summary is machine-generated.

Dynamin, a GTPase, is crucial for cellular processes like endocytosis and organelle division. Its dysfunction is linked to numerous diseases, highlighting its therapeutic potential.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Medicine

Background:

  • Dynamin is a GTPase essential for clathrin-dependent endocytosis and vesicular trafficking.
  • It functions as molecular scissors in vesicle formation and is involved in organelle division, viral resistance, and mitochondrial dynamics.
  • Dynamin's role extends to phagocytosis and mitochondrial fusion/fission.

Purpose of the Study:

  • To review dynamin's mechanisms in various human disorders.
  • To guide medicinal chemists in designing novel dynamin ligands for therapeutic development.

Main Methods:

  • Literature review of dynamin's function and involvement in disease pathophysiology.
  • Analysis of dynamin-related mechanisms in neurological, cardiovascular, and other conditions.

Main Results:

  • Dynamin dysfunction is implicated in Alzheimer's, Parkinson's, Huntington's, and Charcot-Marie-Tooth diseases.
  • It is also linked to heart failure, schizophrenia, epilepsy, cancer, dominant optic atrophy, osteoporosis, and Down's syndrome.
  • The review details dynamin's multifaceted roles in cellular processes and disease.

Conclusions:

  • Understanding dynamin's role in disease is key for developing targeted therapies.
  • Novel dynamin ligands could offer new treatment strategies for a wide range of dynamin-related disorders.