The DOI matches its Crossref record; 65 of the 65 references it cites were found in a registry or an index.
Laminin Polymerization Induces a Receptor–Cytoskeleton Network
Open accessAbstract
The transition of laminin from a monomeric to a polymerized state is thought to be a crucial step in the development of basement membranes and in the case of skeletal muscle, mutations in laminin can result in severe muscular dystrophies with basement membrane defects. We have evaluated laminin polymer and receptor interactions to determine the requirements for laminin assembly on a cell surface and investigated what cellular responses might be mediated by this transition. We found that on muscle cell surfaces, laminins preferentially polymerize while bound to receptors that included dystroglycan and α7β1 integrin. These receptor interactions are mediated through laminin COOH-terminal domains that are spatially and functionally distinct from NH2-terminal polymer binding sites. This receptor-facilitated self-assembly drives rearrangement of laminin into a cell-associated polygonal network, a process that also requires actin reorganization and tyrosine phosphorylation. As a result, dystroglycan and integrin redistribute into a reciprocal network as do cortical cytoskeleton components vinculin and dystrophin. Cytoskeletal and receptor reorganization is dependent on laminin polymerization and fails in response to receptor occupancy alone (nonpolymerizing laminin). Preferential polymerization of laminin on cell surfaces, and the resulting induction of cortical architecture, is a cooperative process requiring laminin– receptor ligation, receptor-facilitated self-assembly, actin reorganization, and signaling events.
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Cites
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Extracellular Matrix Rigidity Causes Strengthening of Integrin–Cytoskeleton Linkages
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Cited by
Form and function: The laminin family of heterotrimers
Colognato, H., & Yurchenco, P. D. (2000) · Developmental Dynamics · doi:10.1002/(sici)1097-0177(200006)218:2<213::aid-dvdy1>3.0.co;2-r · Cited by 1,244
Self-citationBasement Membranes: Cell Scaffoldings and Signaling Platforms
Yurchenco, P. D. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004911 · Cited by 959
Self-citationLAMININ FUNCTIONS IN TISSUE MORPHOGENESIS
Miner, J. H., & Yurchenco, P. D. (2004) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.20.010403.094555 · Cited by 757
Self-citationZenker, M., Aigner, T., Wendler, O., Tralau, T., Müntefering, H., Fenski, R., Pitz, S., Schumacher, V., Royer-Pokora, B., Wühl, E., et al. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh284 · Cited by 498
Integrins as receptors for laminins
Belkin, A. M., & Stepp, M. A. (2000) · Microscopy Research and Technique · doi:10.1002/1097-0029(20001101)51:3<280::aid-jemt7>3.0.co;2-o · Cited by 384
Metadata
- Authors
- Colognato, H., Winkelmann, D. A., & Yurchenco, P. D.
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 1999-05-03
- Volume
- 145
- Issue
- 3
- Pages
- 619-631
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W1994556000
- Cited by
- 302
- References
- 65
- FWCI
- 10.16
- Type
- journal article
- Language
- en
- Open access
- green
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