Caveolae Dynamics in Cellular Signaling

Caveolae are small, flask-shaped invaginations of the plasma membrane enriched in cholesterol, sphingolipids and caveolin proteins. These specialised domains serve as dynamic signalling platforms that integrate mechanical cues, lipid regulation and receptor-mediated endocytosis. Caveolin and cavin family members cooperate to assemble and stabilise caveolae under resting conditions and orchestrate rapid disassembly in response to membrane tension or ligand binding. Within these nano-domains, key signalling molecules—such as kinases, G-proteins and growth factor receptors—are sequestered or released to fine-tune pathways including nitric oxide synthesis, transforming growth factor-β regulation and mTORC1 activation. Aberrant caveolar dynamics have been linked to cardiovascular dysfunction, muscular dystrophies and tumour progression, underscoring their broad physiological importance and therapeutic potential.

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Caveolae Dynamics in Cellular Signaling publication trend

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Technical terms

Caveolae: Small, cholesterol-rich invaginations of the plasma membrane that act as specialised signalling and endocytic microdomains.

Caveolin-1: Integral membrane protein essential for the formation and scaffolding function of caveolae in many cell types.

Caveolin-3: Muscle-specific caveolin isoform that associates with caveolae on the sarcolemma and regulates muscle cell signalling.

Cavins: Peripheral membrane proteins that oligomerise with caveolins to stabilise the caveolar coat and determine its curvature.

Endocytosis: Cellular process by which membrane invaginations internalise extracellular material or receptors for trafficking and signalling.

mTORC1: Mechanistic target of rapamycin complex 1, a kinase assembly that senses nutrient availability to regulate protein synthesis and cell growth.

Scaffolding domain: Cytosolic region of caveolin that binds and organises signalling proteins within caveolae.

References

1. Caveolin-1 mediates the utilization of extracellular proteins for survival in refractory gastric cancer. Experimental & Molecular Medicine (2023).
2. Caveolin‐3 loss linked with the P104L LGMD‐1C mutation modulates skeletal muscle mTORC1 signalling and cholesterol homeostasis. Journal of Cachexia Sarcopenia and Muscle (2023).
3. Single-molecule analysis reveals self assembly and nanoscale segregation of two distinct cavin subcomplexes on caveolae. eLife (2014).
4. Molecular Composition and Ultrastructure of the Caveolar Coat Complex. PLOS Biology (2013).
5. Caveolins, a Family of Scaffolding Proteins for Organizing “Preassembled Signaling Complexes” at the Plasma Membrane*. Journal of Biological Chemistry (1998).
6. Identification of Peptide and Protein Ligands for the Caveolin-scaffolding Domain IMPLICATIONS FOR THE INTERACTION OF CAVEOLIN WITH CAVEOLAE-ASSOCIATED PROTEINS*. Journal of Biological Chemistry (1997).
7. Dissecting the Interaction between Nitric Oxide Synthase (NOS) and Caveolin FUNCTIONAL SIGNIFICANCE OF THE NOS CAVEOLIN BINDING DOMAININ VIVO *. Journal of Biological Chemistry (1997).
8. Caveolin-1 Regulates Transforming Growth Factor (TGF)-β/SMAD Signaling through an Interaction with the TGF-β Type I Receptor*. Journal of Biological Chemistry (2000).
9. Src Tyrosine Kinases, Gα Subunits, and H-Ras Share a Common Membrane-anchored Scaffolding Protein, Caveolin CAVEOLIN BINDING NEGATIVELY REGULATES THE AUTO-ACTIVATION OF Src TYROSINE KINASES*. Journal of Biological Chemistry (1996).