Mical junction series#

Coordination of these cellular functions is especially important, but the precise mechanism remains elusive. Indicate that actinin-4 is involved in recruiting JRAB/MICAL-L2 to cell-cell junctions and forming functional TJs.Дuring epithelial junctional development, both vesicle transport and reorganization of the actin cytoskeleton must be spatiotemporally regulated. This JRAB/MICAL-L2 recruitment as well as the formation of functional TJs was delayed in actinin-4-depleted cells. During the epithelial polarization after replating, JRAB/MICAL-L2 was recruited from the cytosol to cell-cell junctions. Actinin-4 was colocalized with JRAB/MICAL-L2 at cell-cell junctions and linked JRAB/MICAL-L2 to F-actin.ДЄlthough actinin-4 bound to JRAB/MICAL-L2 without Rab13, the actinin-4-JRAB/MICAL-L2 interaction was enhanced by Rab13 activation.Дepletion of actinin-4 by using small interfering RNA inhibited the recruitment of occludin to TJs during the Ca2+ switch. We then identified actinin-4, which was originally isolated as an actin-binding protein associated withД¬ell motility and cancer invasion/metastasis, as a binding protein for the PM-targeting domain of JRAB/MICAL-L2, using a yeast

Mical junction series#

Using a series of deletion mutants, we found the plasma membrane (PM)-targeting domain Mediated the endocytic recycling of the integral TJ protein occludin and the formation of functional TJs. Rab13 and a junctional Rab13-binding protein (JRAB)/molecule interacting with CasL-like 2 (MICAL-L2) localized at TJs and Tight junctions (TJs) are cell-cell adhesive structures that undergo continuous remodeling.