LRBA organizes distinct vesicular trafficking systems in distal nephron segments for water and sodium conservation

Proc Natl Acad Sci U S A. 2026 May 5;123(18):e2525505123. doi: 10.1073/pnas.2525505123. Epub 2026 Apr 28.

Abstract

Lipopolysaccharide-responsive and beige-like anchor protein (LRBA) deficiency is a rare genetic disorder characterized by immune dysregulation. The immune checkpoint molecule cytotoxic T lymphocyte-associated antigen 4 (CTLA-4) fails to perform proper membrane trafficking in the absence of LRBA. In addition to immune cells, LRBA localizes to intracellular vesicles in various epithelial cells; however, its physiological roles have not been accurately deciphered. It was observed in this study that LRBA facilitates water and sodium transport by promoting vesicular trafficking of aquaporin-2 (AQP2) and AQP4 in renal collecting duct cells and that of sterile 20/SPS1-related proline/alanine-rich kinase (SPAK) in distal convoluted tubule cells. Consequently, Lrba knockout mice exhibited vasopressin-resistant polyuria and hypotension under sodium-restricted conditions. This registry study revealed a polyuric phenotype in a subset of patients with LRBA deficiency, characterized by inappropriately low urine specific gravity despite the presence of chronic diarrhea. Notably, desmopressin treatment ameliorated impaired urinary concentration in a mouse model of human LRBA deficiency. LRBA functions as a central coordinator of fluid and sodium homeostasis by organizing segment-specific vesicular trafficking systems in renal epithelial cells.

Keywords: AQPs; LRBA; SPAK; hypotension; polyuria.

MeSH terms

  • Adaptor Proteins, Signal Transducing* / deficiency
  • Adaptor Proteins, Signal Transducing* / genetics
  • Adaptor Proteins, Signal Transducing* / metabolism
  • Animals
  • Aquaporin 2 / genetics
  • Aquaporin 2 / metabolism
  • Humans
  • Kidney Tubules, Collecting / metabolism
  • Mice
  • Mice, Knockout
  • Nephrons* / metabolism
  • Polyuria / genetics
  • Polyuria / metabolism
  • Protein Serine-Threonine Kinases / genetics
  • Protein Serine-Threonine Kinases / metabolism
  • Sodium* / metabolism
  • Water* / metabolism

Substances

  • Sodium
  • Aquaporin 2
  • Adaptor Proteins, Signal Transducing
  • Water
  • Protein Serine-Threonine Kinases
  • Stk39 protein, mouse