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PROSITE documentation PDOC51115 [for PROSITE entry PS51115]

Laminin IV domain profiles





Description

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. The laminins can self-assemble, bind to other matrix macromolecules, and have unique and shared cell interactions mediated by integrins, dystroglycan, and other receptors. Through these interactions, laminins critically contribute to cell differentiation, shape and movement, maintenance of tissue phenotypes, and promotion of tissue survival [1,2].

The different laminin chains share a 600-residue domain I/II which oligomerizes into a rod-like coiled-coil structure forming the long arm of laminins. The N-terminal short arms consist of rod-like elements (domain III and V) formed by tandem arrays of laminin-type EGF modules (see <PDOC00961>) and several globular domains: domains IV and domain VI (laminin N-terminal) (see <PDOC51117>). All α chains share a unique C-terminal G domain which consists of five laminin G modules (see <PDOC50025>) [3]. Laminin IV domain is also found in the perlecan protein, an integral component of basement membranes, which serves also as an attachment substrate for cells, but it is not found in short laminin chains (α4 or β3). The function of this domain is not yet known.

The domain IV of laminin β chains displays no sequence homology to other laminin IV domains, we thus have developed two profiles. The first one recognized all laminin IV domains except the one found in laminin β chains. We have developed a second profile to recognize this atypical domain IV.

Last update:

April 2005 / First entry.

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Technical section

PROSITE methods (with tools and information) covered by this documentation:

LAMININ_IVA, PS51115; Laminin IV type A domain profile  (MATRIX)

LAMININ_IVB, PS51116; Laminin IV type A domain profile  (MATRIX)


References

1AuthorsColognato H. Yurchenco P.D.
TitleForm and function: the laminin family of heterotrimers.
SourceDev. Dyn. 218:213-234(2000).
PubMed ID10842354
DOI10.1002/(SICI)1097-0177(200006)218:2<213::AID-DVDY1>3.0.CO;2-R

2AuthorsYurchenco P.D. Wadsworth W.G.
TitleAssembly and tissue functions of early embryonic laminins and netrins.
SourceCurr. Opin. Cell Biol. 16:572-579(2004).
PubMed ID15363809
DOI10.1016/j.ceb.2004.07.013

3AuthorsSasaki M. Kleinman H.K. Huber H. Deutzmann R. Yamada Y.
TitleLaminin, a multidomain protein. The A chain has a unique globular domain and homology with the basement membrane proteoglycan and the laminin B chains.
SourceJ. Biol. Chem. 263:16536-16544(1988).
PubMed ID3182802



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