A century of warfare shoots holes in anti-Caulerpa campaign

Effort to have all varieties of the marine alga Caulerpa taxifolia listed as noxious weeds hinges on the argument that the alga's proliferation in the Mediterranean Sea is a cause and not a consequence of environmental degradation. Until now, the occurrence of two populations in a pristine part of the northern Mediterranean near the island of Porquerolles has upheld this claim. Here we show that the alga's development at Porquerolles is indeed a consequence of environmental degradation caused by military weapons' impacts on seagrass beds during the last century. The available data show that substratum enrichment plays a key role in fostering development of Caulerpa, irrespective of whether this results directly from pollution or from the impacts of pollution and other anthropogenic factors on benthic vegetation cover

Détermination des radionucléides anthropiques plutonium, neptunium, américium, césium et strontium dans l'environnement marin Méditerranéen

NICE-BU Sciences (060882101) / SudocSudocFranceF

PLEKHA7 Recruits PDZD11 to Adherens Junctions to Stabilize Nectins

PLEKHA7 is a junctional protein implicated in stabilization of the cadherin protein complex, hypertension, cardiac contractility, glaucoma, microRNA processing, and susceptibility to bacterial toxins. To gain insight into the molecular basis for the functions of PLEKHA7, we looked for new PLEKHA7 interactors. Here, we report the identification of PDZ domain-containing protein 11 (PDZD11) as a new interactor of PLEKHA7 by yeast two-hybrid screening and by mass spectrometry analysis of PLEKHA7 immunoprecipitates. We show that PDZD11 (17 kDa) is expressed in epithelial and endothelial cells, where it forms a complex with PLEKHA7, as determined by co-immunoprecipitation analysis. The N-terminal Trp-Trp (WW) domain of PLEKHA7 interacts directly with the N-terminal 44 amino acids of PDZD11, as shown by GST-pulldown assays. Immunofluorescence analysis shows that PDZD11 is localized at adherens junctions in a PLEKHA7-dependent manner, because its junctional localization is abolished by knock-out of PLEKHA7, and is rescued by re-expression of exogenous PLEKHA7. The junctional recruitment of nectin-1 and nectin-3 and their protein levels are decreased via proteasome-mediated degradation in epithelial cells where either PDZD11 or PLEKHA7 have been knocked-out. PDZD11 forms a complex with nectin-1 and nectin-3, and its PDZ domain interacts directly with the PDZ-binding motif of nectin-1. PDZD11 is required for the efficient assembly of apical junctions of epithelial cells at early time points in the calcium-switch model. These results show that the PLEKHA7-PDZD11 complex stabilizes nectins to promote efficient early junction assembly and uncover a new molecular mechanism through which PLEKHA7 recruits PDZ-binding membrane proteins to epithelial adherens junctions