Aquaporine
Aquaporine, often spelled aquaporin, refers to a family of integral membrane proteins that form channels specialized for water transport across cell membranes. They are found in bacteria, plants, and animals and regulate osmoregulation and hydration. Some members also conduct small solutes such as glycerol, in which case they are called aquaglyceroporins.
Structure and mechanism: Each aquaporin monomer folds into six helices and assembles as a tetramer in the
Function and regulation: Water transport via aquaporins follows osmotic gradients and is typically faster than simple
Diversity and distribution: Humans express thirteen aquaporins (AQP0–AQP12) with tissue-specific patterns, including AQP1 in kidney and
Clinical relevance: Altered aquaporin function can cause disease. AQP2 mutations cause nephrogenic diabetes insipidus; AQP0 defects
Discovery and nomenclature: Aquaporins were identified in 1992 by Peter Agre and colleagues, who later shared