LAMB1
Domain
The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.
Domains VI and IV are globular.
Function
Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Involved in the organization of the laminar architecture of cerebral cortex. It is probably required for the integrity of the basement membrane/glia limitans that serves as an anchor point for the endfeet of radial glial cells and as a physical barrier to migrating neurons. Radial glial cells play a central role in cerebral cortical development, where they act both as the proliferative unit of the cerebral cortex and a scaffold for neurons migrating toward the pial surface.
Involvement in disease
Lissencephaly 5
LIS5
An autosomal recessive brain malformation characterized by cobblestone changes in the cortex, more severe in the posterior region, and subcortical band heterotopia. Affected individuals have hydrocephalus, seizures, and severely delayed psychomotor development.
None
The disease is caused by variants affecting the gene represented in this entry.
Cellular localization
- Secreted
- Extracellular space
- Extracellular matrix
- Basement membrane
- Major component.
Alternative names
Laminin subunit beta-1, Laminin B1 chain, Laminin-1 subunit beta, Laminin-10 subunit beta, Laminin-12 subunit beta, Laminin-2 subunit beta, Laminin-6 subunit beta, Laminin-8 subunit beta, LAMB1