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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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Assembly of Cytoskeletal Filaments01:18

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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 addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
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Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
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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.
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Related Experiment Video

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Multiprotein Assemblies, Phosphorylation and Dephosphorylation in Neuronal Cytoskeleton.

Natalya Kurochkina1, Matthew R Sapio2, Michael J Iadarola2

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|July 28, 2023
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Mutations in Breast cancer associated protein 1/BRCA1-associated RING domain 1 (BRCA1/BARD1) ankyrin repeats correlate with kinase phosphorylation sites. This suggests a role for these mutations in Alzheimer disease pathogenesis and offers potential drug targets.

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Area of Science:

  • Cellular biology
  • Neuroscience
  • Biochemistry

Background:

  • Filament systems regulate cell shape and dynamics, with neurofilament assembly dependent on kinase phosphorylation.
  • Breast cancer associated protein 1 (BRCA1)/BRCA1-associated RING domain 1 (BARD1) pathways are implicated in Alzheimer disease (AD) pathogenesis.
  • BRCA1 accumulation and colocalization with tau aggregates in AD patients suggest involvement of mutant BRCA1/BARD1 proteins.

Approach:

  • Investigated the correlation between mutation locations in BARD1 ankyrin repeats and Cdk5 phosphorylation motifs.
  • Mapped mutation sites onto the protein's 3D structure and analyzed backbone dihedral angles.
  • Examined conformational transitions between helical and extended conformations in ankyrin repeat sequences.

Key Points:

  • Mutation sites in BARD1 ankyrin repeats show a strong correlation with Cdk5 phosphorylation motifs.
  • Mutations cluster near helix N-termini with T/SXXH motifs, facilitating conformational transitions.
  • These transitions may be crucial for substrate interaction with kinase active sites.

Conclusions:

  • The location of mutations within BARD1 ankyrin repeats influences phosphorylation patterns.
  • Conformational changes induced by mutations could underlie BRCA1/BARD1 involvement in AD.
  • BARD1 ankyrin repeats are potential targets for novel therapeutic strategies in neurodegenerative diseases.