Laminin Functions in Extracellular Matrix Biology

Laminins are heterotrimeric glycoproteins that form a fundamental scaffold within the extracellular matrix, particularly in basement membranes. Each laminin molecule comprises α, β and γ chains arranged into a characteristic cross-shaped structure, with short-arm globular domains mediating network assembly and a long coiled-coil region terminating in cell-adhesive globular modules. Through polymerisation, laminins establish a planar lattice that anchors cells by engaging surface receptors and growth factors, thereby regulating cell adhesion, migration, proliferation and differentiation. Isoform diversity among laminin subunits underpins tissue specificity and developmental cues, from embryogenesis and stem cell fate decisions to tissue homeostasis. Mechanical resilience and dynamic adaptability of laminin networks contribute to wound healing and organ integrity, while genetic or post-translational perturbations in laminin assembly underlie a spectrum of human disorders. The multifunctional nature of laminins has inspired bioengineered matrices for regenerative medicine and biomimetic materials for studying cell–matrix interactions under controlled conditions.

Research from Nature Portfolio

High-resolution structural studies have elucidated the atomic basis of laminin polymerisation and its defects in disease. Cryo-electron microscopy of the trimeric laminin α1β1γ1 node at near-atomic resolution revealed calcium-dependent interfaces that drive lattice formation and highlighted how specific mutations disrupt polymer assembly, manifesting as congenital lamininopathies. Complementary integration of cryo-EM with artificial intelligence-guided modelling has enabled systematic analysis of pathogenic polymer nodes, proposing a new classification of lamininopathies and guiding rational design of therapeutic agents aimed at restoring basement membrane integrity.

Laminin Functions in Extracellular Matrix Biology publication trend

The graph below shows the total number of articles in laminin functions in extracellular matrix biology across all publications each year (not limited to Nature Index journals).

Technical terms

Laminin: Heterotrimeric glycoproteins that self-assemble into networks within the extracellular matrix to support tissue structure and function.

Extracellular matrix (ECM): A complex network of proteins and polysaccharides that provides structural support and biochemical cues to cells.

Basement membrane: A specialised form of ECM that underlies epithelial and endothelial cells, acting as a selective barrier and scaffold.

Polymerisation: The process by which individual protein subunits assemble into ordered, higher-order structures or networks.

Isoform: A variant of a protein arising from different gene subunits or alternative splicing, often with distinct functional properties.

Cryo-electron microscopy (cryo-EM): A technique that visualises biomolecules at near-atomic resolution by flash-freezing samples and imaging with electron beams.

References

1. Laminin–Dynamic Bonds Enable Multifunctionality in a Biological 2D Network. Advanced Functional Materials (2023).
2. Cryo-EM reveals the molecular basis of laminin polymerization and LN-lamininopathies. Nature Communications (2023).
3. Interleukin-6 trans-signaling induced laminin switch contributes to reduced trans-endothelial migration of granulocytic cells. Atherosclerosis (2023).
4. Observing Dynamic Conformational Changes within the Coiled-Coil Domain of Different Laminin Isoforms Using High-Speed Atomic Force Microscopy. International Journal of Molecular Sciences (2024).
5. Artificial intelligence and the analysis of cryo-EM data provide structural insight into the molecular mechanisms underlying LN-lamininopathies. Scientific Reports (2023).