BioPAX pathway converted from "Laminin-111 binds collagen type IV" in the Reactome database. Laminin-111 binds collagen type IV Laminin-111 binds collagen type IV Type IV collagen (Yurchenco & Furthmayr 1984) and laminin (Yurchenco et al. 1985,1992, Cheng et al. 1997) can self-assemble in vitro, forming lattice-like polymeric networks which resemble laminin-collagen matrices observed in vivo (Timpl & Brown 1996). Purified laminins are the only basement membrane component able to assemble on cell surfaces in the absence of other components (McKee et al. 2007). Laminin knockouts prevent basement membrane assembly, arresting development at a much earlier stage than knockouts of other ECM components such as collagen IV, nidogens (entactin), perlecan or agrin (Yurchenko et al. 2004). This suggests a regulatory function for the laminin network. Laminin molecules bind to each other in a three-way interaction involving the LN domains located at the end of the three short arms. Each interaction involves one each of alpha, beta and gamma laminin subunits (Yurchenko & Cheng 1993, McKee et al. 2007) forming a polygonal structure (Yurchenko et al. 1992). <br><br>In the basement membrane collagen type IV and laminin are found in an approximately 1:1 molar ratio (Kleinman et al. 1986). Binding between laminin and collagen type IV is primarily facilitated by nidogen (Aumailley et al. 1989, Fox et al. 1991), but direct binding has been observed (Charonis et al. 1985, Rao et al. 1985). Laminin-111 (laminin-1) binds to type IV collagen through its short arms (Laurie et al. 1986). Authored: Jupe, S, 2012-08-08 Reviewed: Yamada, K, Humphries, MJ, Hynes, R, 2008-05-07 08:53:37 Reviewed: Ricard-Blum, Sylvie, 2013-08-13 Edited: Jupe, S, 2013-08-13 Converted from EntitySet in Reactome Reactome DB_ID: 2564668 1 extracellular region GO 0005576 Collagen IV [extracellular region] Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntity Reactome http://www.reactome.org Reactome DB_ID: 215989 1 Laminin-111 [extracellular region] Laminin-111 Laminin-1 Reactome DB_ID: 215959 1 UniProt:P07942 LAMB1 LAMB1 LAMB1 FUNCTION Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Involved in the organization of the laminar architecture of cerebral cortex. It is probably required for the integrity of the basement membrane/glia limitans that serves as an anchor point for the endfeet of radial glial cells and as a physical barrier to migrating neurons. Radial glial cells play a central role in cerebral cortical development, where they act both as the proliferative unit of the cerebral cortex and a scaffold for neurons migrating toward the pial surface.SUBUNIT Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Beta-1 is a subunit of laminin-1 (laminin-111 or EHS laminin), laminin-2 (laminin-211 or merosin), laminin-6 (laminin-311 or K-laminin), laminin-8 (laminin-411), laminin-10 (laminin-511) and laminin-12 (laminin-213). Interacts with ITGB1 (By similarity).DOMAIN The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.DOMAIN Domains VI and IV are globular. Homo sapiens NCBI Taxonomy 9606 UniProt P07942 Chain Coordinates 22 EQUAL 1786 EQUAL Reactome DB_ID: 215962 1 UniProt:P11047 LAMC1 LAMC1 LAMB2 LAMC1 FUNCTION Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.SUBUNIT Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Gamma-1 is a subunit of laminin-1 (laminin-111 or EHS laminin), laminin-2 (laminin-211 or merosin), laminin-3 (laminin-121 or S-laminin), laminin-4 (laminin-221 or S-merosin), laminin-6 (laminin-311 or K-laminin), laminin-7 (laminin-321 or KS-laminin), laminin-8 (laminin-411), laminin-9 (laminin-421), laminin-10 (laminin-511) and laminin-11 (laminin-521).TISSUE SPECIFICITY Found in the basement membranes (major component).DOMAIN The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.DOMAIN Domains VI and IV are globular. UniProt P11047 34 EQUAL 1609 EQUAL Reactome DB_ID: 215953 1 UniProt:P25391 LAMA1 LAMA1 LAMA1 LAMA FUNCTION Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.SUBUNIT Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Alpha-1 is a subunit of laminin-1 (laminin-111 or EHS laminin) and laminin-3 (laminin-121 or S-laminin).DOMAIN The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.DOMAIN Domains VI, IV and G are globular.PTM Tyrosine phosphorylated by PKDCC/VLK. UniProt P25391 18 EQUAL 3075 EQUAL Reactome Database ID Release 83 215989 Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=215989 Reactome R-HSA-215989 1 Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-215989.1 Reactome DB_ID: 2426371 1 Collagen type IV network:Laminin-1 [extracellular region] Collagen type IV network:Laminin-1 Converted from EntitySet in Reactome Reactome DB_ID: 2564668 1 Reactome DB_ID: 215989 1 Reactome Database ID Release 83 2426371 Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=2426371 Reactome R-HSA-2426371 1 Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-2426371.1 Reactome Database ID Release 83 2328145 Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=2328145 Reactome R-HSA-2328145 1 Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-2328145.1 1577869 Pubmed 1992 Laminin forms an independent network in basement membranes Yurchenco, P D Cheng, Y S Colognato, H J. Cell Biol. 117:1119-33 3997891 Pubmed 1985 Laminin polymerization in vitro. Evidence for a two-step assembly with domain specificity Yurchenco, P D Tsilibary, E C Charonis, A S Furthmayr, H J. Biol. Chem. 260:7636-44 14996432 Pubmed 2004 Basement membrane assembly, stability and activities observed through a developmental lens Yurchenco, Peter D Amenta, Peter S Patton, Bruce L Matrix Biol. 22:521-38 1717261 Pubmed 1991 Recombinant nidogen consists of three globular domains and mediates binding of laminin to collagen type IV Fox, J W Mayer, U Nischt, R Aumailley, M Reinhardt, D Wiedemann, H Mann, K Timpl, R Krieg, T Engel, J EMBO J. 10:3137-46 8851045 Pubmed 1996 Supramolecular assembly of basement membranes Timpl, R Brown, J C Bioessays 18:123-32 2937447 Pubmed 1986 Basement membrane complexes with biological activity Kleinman, H K McGarvey, M L Hassell, J R Star, V L Cannon, F B Laurie, G W Martin, G R Biochemistry 25:312-8 2506015 Pubmed 1989 Binding of nidogen and the laminin-nidogen complex to basement membrane collagen type IV Aumailley, M Wiedemann, H Mann, K Timpl, R Eur. J. Biochem. 184:241-8 8349613 Pubmed 1993 Self-assembly and calcium-binding sites in laminin. A three-arm interaction model Yurchenco, P D Cheng, Y S J. Biol. Chem. 268:17286-99 3921025 Pubmed 1985 Binding domain for laminin on type IV collagen Rao, C N Margulies, I M Liotta, L A Biochem. Biophys. Res. Commun. 128:45-52 6722126 Pubmed 1984 Self-assembly of basement membrane collagen Yurchenco, PD Furthmayr, H Biochemistry 23:1839-50 2946868 Pubmed 1986 Localization of binding sites for laminin, heparan sulfate proteoglycan and fibronectin on basement membrane (type IV) collagen Laurie, G W Bing, J T Kleinman, H K Hassell, J R Aumailley, M Martin, G R Feldmann, R J J. Mol. Biol. 189:205-16 3997977 Pubmed 1985 Binding of laminin to type IV collagen: a morphological study Charonis, AS Tsilibary, EC Yurchenco, PD Furthmayr, H J Cell Biol 100:1848-53 17517882 Pubmed 2007 Role of laminin terminal globular domains in basement membrane assembly McKee, Karen K Harrison, David Capizzi, Stephanie Yurchenco, Peter D J. Biol. Chem. 282:21437-47 9395489 Pubmed 1997 Self-assembly of laminin isoforms Cheng, Y S Champliaud, M F Burgeson, R E Marinkovich, M P Yurchenco, P D J. Biol. Chem. 272:31525-32 9989793 Pubmed 1999 NC1 domain of type VII collagen binds to the beta3 chain of laminin 5 via a unique subdomain within the fibronectin-like repeats Chen, M Marinkovich, M P Jones, J C O'Toole, E A Li, Y Y Woodley, D T J. Invest. Dermatol. 112:177-83 9245798 Pubmed 1997 Laminin 5 binds the NC-1 domain of type VII collagen Rousselle, P Keene, D R Ruggiero, F Champliaud, M F Rest, M Burgeson, R E J. Cell Biol. 138:719-28