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Review
. 2010 Jan;28(1):79-87.
doi: 10.1016/j.det.2009.10.009.

Adhesion and migration, the diverse functions of the laminin alpha3 subunit

Kevin J Hamill  1 , Amy S Paller, Jonathan C R Jones
Affiliations
Review

Adhesion and migration, the diverse functions of the laminin alpha3 subunit

Kevin J Hamill et al. Dermatol Clin. 2010 Jan.

Abstract

The laminins are a secreted family of heterotrimeric molecules essential for basement membrane formation, structure, and function. It is now well established that the alpha3 subunit of laminins-332, -321, and -311 plays an important role in mediating epidermal-dermal integrity and is essential for the skin to withstand mechanical stresses. These laminins also regulate cell migration and mechanosignal transduction. This article provides an overview of the gene, transcripts, and protein structures of laminin alpha3. Also discussed are the proposed functions for the alpha3 subunit-containing laminins.

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Figures

Figure 1
Figure 1
A) Genomic organization of LAMA3 gene, vertical bars represent exons, horizontal line introns. B) LAMA3A and LAMA3B transcript organization; blue exons – common to both transcripts, orange -specific to LAMA3A, grey – specific to LAMA3B, pink – specific to LAMA3B2, Below each transcript is a diagrammatic representation of the domain architecture; LN – laminin N terminal domain, LE – laminin-type epidermal growth factor-like repeats, L4 – globular domain, LCC – laminin coiled coil domain, LG laminin globular domains. C) Laminin α3 containing heterotrimer structure. Color scheme of conserved domains as in B, with purple - Lβ-laminin β chain globular domain. Arrows in LM332 and LM3B32 indicate processing points discussed in the text.
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