VAPA-dependent lipid transport at ER-lamellar body contact sites promotes human lung surfactant formation.

A homozygous nonsense VAPA variant (p.(Glu12 ∗ )) in a patient is linked to progressive surfactant dysfunction, cholesterol pneumonitis, and pulmonary fibrosis.

• Why it matters: Tissue-specific VAP functions at ER membrane contact sites are unclear, limiting understanding of how disrupted lipid trafficking contributes to syndromic lung disease.
• What they did: The study analyzed human alveolar type 2 cells with an N-terminally truncated VAPA that partially bypasses the stop codon, and mapped VAPA’s interaction with ABCA3.
• The result: VAPA-ABCA3 promotes lipid exchange at ER–lamellar body contact sites, and this MCS function is lost with VAPA truncation, defining a surfactant lipid trafficking pathway.

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