title: Mammalian tolloid proteinases: role in growth factor signalling.
abstract: Tolloid proteinases are essential for tissue patterning and extracellular matrix assembly. The members of the family differ in their substrate specificity and activity, despite sharing similar domain organization. The mechanisms underlying substrate specificity and activity are complex, with variation between family members, and depend on both multimerization and substrate interaction. In addition, enhancers, such as Twisted gastrulation (Tsg), promote cleavage of tolloid substrate, chordin, to regulate growth factor signalling. Although Tsg and mammalian tolloid (mTLD) are involved in chordin cleavage, no interaction has been detected between them, suggesting Tsg induces a change in chordin to increase susceptibility to cleavage. All members of the tolloid family bind the N terminus of latent TGFβ-binding protein-1, providing support for their role in TGFβ signalling.
authors.affiliation: Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, UK.
authors.forename: Helen
authors.initials: H
authors.lastname: Troilo
authors.affiliation: Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, UK.
authors.forename: Christopher P
authors.initials: CP
authors.lastname: Bayley
authors.affiliation: Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, UK.
authors.forename: Anne L
authors.initials: AL
authors.lastname: Barrett
authors.affiliation: Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, UK.|Beamline B21, Diamond Light Source, Harwell Science & Innovation Campus, Didcot, Oxfordshire, UK.
authors.forename: Michael P
authors.initials: MP
authors.lastname: Lockhart-Cairns
authors.affiliation: Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, UK.
authors.forename: Thomas A
authors.initials: TA
authors.lastname: Jowitt
authors.affiliation: Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, UK.
authors.forename: Clair
authors.initials: C
authors.lastname: Baldock
mesh_terms: D000818:Animals; D006023:Glycoproteins / Q000235:genetics / Q000378:metabolism; D006801:Humans; D036341:Intercellular Signaling Peptides and Proteins / Q000235:genetics / Q000378:metabolism; D053779:Latent TGF-beta Binding Proteins / Q000235:genetics*; D008322:Mammals / Q000235:genetics; D051379:Mice; D010447:Peptide Hydrolases / Q000235:genetics*; D011506:Proteins / Q000235:genetics; D015398:Signal Transduction; D013379:Substrate Specificity; D055394:Tolloid-Like Metalloproteinases / Q000235:genetics*; D053773:Transforming Growth Factor beta1 / Q000235:genetics*
chemical_list: D006023:Glycoproteins; D036341:Intercellular Signaling Peptides and Proteins; C509032:LTBP1 protein, human; D053779:Latent TGF-beta Binding Proteins; D011506:Proteins; C508960:TGFB1 protein, human; D053773:Transforming Growth Factor beta1; C473561:twisted gastrulation protein, mouse; C054234:chordin; D010447:Peptide Hydrolases; D055394:Tolloid-Like Metalloproteinases
keywords: BMP signalling; chordin; latent TGFβ-binding protein; twisted gastrulation