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Related Concept Videos

Cytoskeletal Accessory Proteins01:13

Cytoskeletal Accessory Proteins

The cytoskeleton is an essential cell component that plays several structural and functional roles. However, the filaments that make up the cytoskeleton cannot function independently and depend on the accessory or ancillary proteins to effectively carry out their function. Accessory proteins associate with cytoskeletal filaments and their monomers, aiding filament formation and function. They also help in the cross-communication among cytoskeletal filaments. Cytoskeletal accessory proteins are...
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Interaction domains in cell signaling
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Intracellular Signaling Affects Focal Adhesions01:17

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High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis
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Published on: October 15, 2019

S100-annexin complexes--structural insights.

Anne C Rintala-Dempsey1, Atoosa Rezvanpour, Gary S Shaw

  • 1Department of Biochemistry, University of Western Ontario, London, Canada.

The FEBS Journal
|September 18, 2008
PubMed
Summary
This summary is machine-generated.

Calcium-binding proteins annexins and S100 proteins interact through diverse mechanisms. These interactions, involving N-terminal or core regions, are crucial for cellular functions like membrane fusion.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Annexins and S100 proteins are distinct calcium-binding protein families.
  • Annexins bind phospholipids via their helical core domain.
  • Calcium binding can expose N-terminal regions of some annexins for interaction.

Purpose of the Study:

  • To elucidate the structural mechanisms of S100-annexin interactions.
  • To understand the diversity of recognition modes between these protein families.
  • To explore the role of these interactions in cellular processes like membrane fusion.

Main Methods:

  • Structural studies of S100-annexin complexes.
  • Analysis of protein-protein binding interfaces.
  • Investigating calcium-dependent conformational changes.

Main Results:

  • Specific S100-annexin interactions involve annexin N-termini.
  • Some interactions are more complex, engaging the annexin core domain.
  • Multiple recognition modes exist between S100 proteins and annexins.

Conclusions:

  • S100-annexin interactions are diverse, utilizing different protein regions.
  • These interactions may facilitate membrane fusion by bridging annexin-bound membranes.
  • Understanding these complexes offers insights into protein-protein recognition mechanisms.