Mammalian tolloid proteinases: role in growth factor signalling

DOI: 10.1002/1873-3468.12287

Authors: Helen Troilo (Wellcome Trust Centre for Cell-Matrix Research, University of Manchester) , Christopher P. Bayley (Wellcome Trust Centre for Cell-Matrix Research, University of Manchester) , Anne L. Barrett (Wellcome Trust Centre for Cell-Matrix Research, University of Manchester) , Michael P. Lockhart-Cairns (University of Manchester; Diamond Light Source) , Thomas A. Jowitt (Wellcome Trust Centre for Cell-Matrix Research, University of Manchester) , Clair Baldock (Wellcome Trust Centre for Cell-Matrix Research, University of Manchester)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Febs Letters , VOL 590 , PAGES 2398 - 2407

State: Published (Approved)
Published: August 2016

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.

Journal Keywords: BMP signalling; chordin; latent TGFβ-binding protein; twisted gastrulation

Subject Areas: Biology and Bio-materials


Technical Areas:

Added On: 01/10/2016 03:15

Documents:
Troilo_et_al-2016-FEBS_Letters.pdf

Discipline Tags:

Structural biology Biophysics Life Sciences & Biotech

Technical Tags: