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Mammalian tolloid proteinases: role in growth factor signalling
Author(s) -
Troilo Helen,
Bayley Christopher P.,
Barrett Anne L.,
LockhartCairns Michael P.,
Jowitt Thomas A.,
Baldock Clair
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12287
Subject(s) - chordin , microbiology and biotechnology , cleavage (geology) , signalling , biology , enhancer , plasma protein binding , chemistry , transcription factor , genetics , gastrulation , gene , embryo , embryogenesis , paleontology , fracture (geology)
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 TGF β‐binding protein‐1, providing support for their role in TGF β signalling.