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Related Concept Videos

Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

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Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
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Mechanisms of Membrane Domain Formation00:59

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Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
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Assembly of Complex Microtubule Structures01:32

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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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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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Actin is a family of globular proteins that are highly abundant in eukaryotic cells. It makes up approximately 1-5% of total cell protein concentration. Actin monomers polymerize to form a complex network of polarized filaments, the actin cytoskeleton, that plays a crucial role in many cellular processes, including cell motility, division, endocytosis, and metastasis of cancer cells.
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Related Experiment Video

Updated: Sep 19, 2025

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
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Membrane-Associated Self-Assembly for Cellular Decision Making.

Samuel L Foley1, Margaret E Johnson1

  • 1T. C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, Maryland, USA.

Arxiv
|June 5, 2025
PubMed
Summary

Molecular self-assembly on surfaces acts as a sensitive switch for detecting cell receptors. This passive mechanism offers a tunable and robust alternative to active cellular signaling pathways.

Area of Science:

  • Biophysics
  • Cellular Biology
  • Biochemistry

Background:

  • Cellular decision-making relies on transmembrane receptors transmitting external signals.
  • Receptor signaling typically involves irreversible, energy-dependent biochemical reactions.
  • Existing passive detection mechanisms lack the sensitivity of active pathways.

Purpose of the Study:

  • To investigate spontaneous molecular self-assembly as a tunable and robust switch for receptor detection.
  • To compare the sensitivity of self-assembly mechanisms with passive and active receptor detection methods.
  • To develop a theoretical framework for understanding self-assembly-based cellular switches.

Main Methods:

  • Derivation of analytical expressions for critical receptor densities.

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  • Utilizing equilibrium stochastic reaction-diffusion simulations.
  • Comparing theoretical predictions with simulation results.

    • Main Results:

    • Spontaneous molecular self-assembly can function as a sensitive switch for receptor detection at physiological concentrations.
    • This self-assembly mechanism demonstrates higher sensitivity compared to other passive detection methods.
    • Analytical expressions accurately predict the critical receptor densities for assembly nucleation and growth.

    Conclusions:

    • Molecular self-assembly provides a sensitive, tunable, and robust mechanism for cellular signal detection.
    • The developed theory offers insights into controlling decision thresholds and response magnitudes.
    • This passive mechanism presents a viable alternative to energy-consuming active signaling pathways.