|PROSITE documentation PDOC51117 [for PROSITE entry PS51117]|
Laminin is a large molecular weight glycoprotein present only in basement membranes in almost every animal tissue. Each laminin is a heterotrimer assembled from α, β and γ chain subunits, secreted and incorporated into cell-associated extracellular matrices .
Basement membrane assembly is a cooperative process in which laminins polymerize through their N-terminal domain (LN or domain VI) and anchor to the cell surface through their G domains (see <PDOC50025>). Netrins may also associate with this network through heterotypic LN domain interactions . This leads to cell signaling through integrins and dystroglycan (and possibly other receptors) recruited to the adherent laminin. This LN domain dependent self-assembly is considered to be crucial for the integrity of basement membranes, as highlighted by genetic forms of muscular dystrophy containing the deletion of the LN module from the α 2 laminin chain .
The laminin N-terminal domain is found in all laminin and netrin subunits except laminin α 3A, α 4 and γ 2.
The profile we developed covers the whole laminin N-terminal domain.Last update:
April 2005 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Colognato H. Yurchenco P.D.|
|Title||Form and function: the laminin family of heterotrimers.|
|Source||Dev. Dyn. 218:213-234(2000).|
|2||Authors||Yurchenco P.D. Cheng Y.S.|
|Title||Self-assembly and calcium-binding sites in laminin. A three-arm interaction model.|
|Source||J. Biol. Chem. 268:17286-17299(1993).|
|3||Authors||Xu H. Wu X.R. Wewer U.M. Engvall E.|
|Title||Murine muscular dystrophy caused by a mutation in the laminin alpha 2 (Lama2) gene.|
|Source||Nat. Genet. 8:297-302(1994).|