Juha Saharinen

TL;DR: LTBPs have a dual function, they are required both for the secretion of the small latent TGF-beta complex as well as directing bound latent T GF-beta to extracellular matrix microfibrils, however, it is not known at present whether LTBPs are capable of forming microFibrils independently, whether they are a part of the fibrillin-containing fibrils.

TL;DR: Molecular modeling of the 8-Cys repeats revealed a hydrophobic interaction surface and lack of three stabilizing hydrogen bonds introduced by the TGF-beta binding motif necessary for the formation of the T GF-beta*LAP - 8- cys repeat complex inside the cells.

TL;DR: The data indicate that an 8‐Cys repeat of LTBP is capable of covalent and specific protein‐protein interactions, and is the first demonstration of an extracellular protein module that is able to exchange cysteine disulfide bonds with heterologous ligand proteins.

TL;DR: The severe neurological phenotype observed in IOSCA, a result of only a single amino acid substitution in Twinkle and Twinky, suggests that these proteins play a crucial role in the maintenance and/or function of specific affected neuronal subpopulations.