Coparenting and Toddler's Interactive Styles in Family Coalitions

The current study examined the coparenting and toddler's interactive styles in family coalitions. According to structural family theory, boundaries between generations are clear in alliances, but disturbed in coalitions: the parents look to the child to regulate their conflictual relationship and the child attempts to meet this need. In a normative sample studied longitudinally during the Lausanne Trilogue Play situation (LTP, N=38), 15 coalition cases were detected. Styles of coparenting and of child's interactions were determined and compared in coalition and alliance cases at 18 months. Findings confirm the structural family model by showing the specific ways in which the coparenting and the toddler's interactive styles are associated in 3 different patterns of coalitions: binding, detouring, and triangulation. They illustrate how the child's triangular capacity, or her ability to simultaneously communicate with both parents, is used to regulate the parents' relationship. They suggest that the LTP observational paradigm is a promising assessment method of early family interactions. They point to the importance of assessing early the child's contribution to family coalitions.

Mutations leading to X-linked hypohidrotic ectodermal dysplasia affect three major functional domains in the tumor necrosis factor family member ectodysplasin-A.

Mutations in the epithelial morphogen ectodysplasin-A (EDA), a member of the tumor necrosis factor (TNF) family, are responsible for the human disorder X-linked hypohidrotic ectodermal dysplasia (XLHED) characterized by impaired development of hair, eccrine sweat glands, and teeth. EDA-A1 and EDA-A2 are two splice variants of EDA, which bind distinct EDA-A1 and X-linked EDA-A2 receptors. We identified a series of novel EDA mutations in families with XLHED, allowing the identification of the following three functionally important regions in EDA: a C-terminal TNF homology domain, a collagen domain, and a furin protease recognition sequence. Mutations in the TNF homology domain impair binding of both splice variants to their receptors. Mutations in the collagen domain can inhibit multimerization of the TNF homology region, whereas those in the consensus furin recognition sequence prevent proteolytic cleavage of EDA. Finally, a mutation affecting an intron splice donor site is predicted to eliminate specifically the EDA-A1 but not the EDA-A2 splice variant. Thus a proteolytically processed, oligomeric form of EDA-A1 is required in vivo for proper morphogenesis.