tolloidBMP1like

TolloidBMP1like, often referred to as the tolloid/BMP1-like family, denotes a group of secreted metalloproteases that belong to the astacin superfamily. This family encompasses tolloid-like and BMP1-like proteins found across metazoans, including vertebrate representatives such as BMP1 and the tolloid-like proteases TLL1 and TLL2, as well as homologs in invertebrates. Members share a characteristic domain architecture that supports extracellular proteolysis: a signal peptide and propeptide, followed by non-catalytic modules such as CUB and EGF-like repeats, and culminating in a C-terminal astacin protease domain. The catalytic site contains the zinc-binding motif essential for metalloprotease activity.

Functionally, tolloidBMP1like proteases are zinc-dependent enzymes that modify the extracellular matrix and regulate signaling pathways. They cleave procollagens to enable proper collagen maturation and fiber assembly, contributing to tissue remodeling and skeletal development. They also process extracellular regulators of BMP signaling, such as chordin, thereby modulating BMP pathway activity during embryogenesis and organogenesis.

Evolutionarily, the tolloid/BMP1-like family shows diversification through gene duplication, yielding multiple paralogs in vertebrates (for example, BMP1, TLL1, TLL2) and various homologs in other animal lineages. This diversification supports the broad involvement of these proteases in ECM dynamics and BMP-related signaling across tissues.

Clinical and research relevance centers on their roles in development, tissue remodeling, and potential involvement in ECM-related disorders. In model systems, perturbations of BMP1-like proteases can affect skeletal formation and connective tissue integrity, underscoring their conserved biological importance.