Claudin and membrane-domain assignments agree with structural junctional participation; direct target localization refines the generic membrane compartment.

The exact donor O88551 is mouse Cldn1, with direct experimental junctional, adhesion and self-binding records. These are family transfers, not mislabeled Cldn16 ortholog assays.

The original PTN000243505 compartment and PTN002634415 transport/channel assertions are preserved. Current experimental grounding is documented separately from uninspected historical node placement.

Q925N4 is mouse Cldn16, with experimental renal absorption and paracellular transport grounding; the linked Ensembl product is preserved as supplied.

The positive ion-transport premise is retained, but the logical process inference carries a membrane-crossing scope that is better represented by paracellular transport.

The current ARBA00027156 set 5 matches the target FunFam and Metazoa and assigns tight-junction localization.

Combined ortholog, domain, subcellular-vocabulary and ARBA mappings support junctional localization and paracellular transport; current rule objects are not treated as reconstructed historical executions.

The original authentic abstract links paracellin-1 to renal tight junctions and magnesium resorption. It supports the biological context but does not resolve the specific intracellular-cation assertion without the unavailable full text.

Human CLDN16 terminal peptides bind ZO-1 PDZ domains, and HA-CLDN16 associates with endogenous canine ZO-1 in MDCK cells. T233R disrupts terminal binding and junctional targeting; the active human construct starts at the second historical methionine.

Human and mouse constructs are tested in epithelial monolayers with dilution-potential and ion-substitution measurements. The active short human construct changes paracellular cation permeability, while the historical longer construct differs in localization.

Wild-type human CLDN16 reaches MDCK-C7 junctions and increases directly measured magnesium permeability. Disease variants separate intracellular retention from impaired function despite junctional localization.

Human CLDN16 and CLDN19 interact and form a cation-selective junctional complex. CLDN16 alone does not produce fibroblast strands, but incorporates into CLDN19-containing strands; the LLC-PK1 selectivity results are model-specific.

Mouse knockdown experiments show reciprocal dependence of CLDN16 and CLDN19 junctional localization and renal divalent-cation handling. The interaction panel supports selective association; exact modern product boundaries are not newly reconstructed from the inspected text.

Explicit mouse CLDN14 and human CLDN16/19 constructs support CLDN14–CLDN16 two-hybrid and reciprocal coimmunoprecipitation results. CLDN14 reduces CLDN16-dependent cation permeability in LLC-PK1 cells; the older oligomer model remains assay-scoped.

Human fluorescent CLDN16/19 constructs show cis association and cooperative contact enrichment, with weak CLDN16 homomeric FRET. Mouse and rat TAL mosaics and mouse segment physiology are distinct from these heterologous human construct assays.

Human CLDN16/19 constructs form heteromeric complexes in cellular and detergent-extracted systems; interface perturbations couple association to junctional selectivity. The results do not determine an atomic native junctional structure or universal stoichiometry.

Dog CLDN16 and CLDN19 reconstituted in claudin-deficient MDCKII cells generate channels with substantial magnesium and calcium permeability. Endogenous CLDN16 and partner-dependent assembly are important controls; the separate CLDN4/8 FRET experiment is not assigned to CLDN16.

Heterologous junctional models support replacement of CLDN16 by CLDN14 within CLDN19-containing structures, alongside mouse kidney observations. The inspected construct section does not explicitly identify every CLDN16 transgene species or accession; host-cell identity is not used as protein-species evidence.