PROSITE documentation PDOC51117Laminin N-terminal (LN) domain profile
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 [1].
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 [2]. 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 [3].
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). | |
| PubMed ID | 10842354 | |
| DOI | 10.1002/(SICI)1097-0177(200006)218:2<213::AID-DVDY1>3.0.CO;2-R |
| 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). | |
| PubMed ID | 8349613 |
| 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). | |
| PubMed ID | 7874173 | |
| DOI | 10.1038/ng1194-297 |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.
View entry in original PROSITE document format
View entry in raw text format (no links)