IQUIFIB   02644
INSTITUTO DE QUIMICA Y FISICOQUIMICA BIOLOGICAS "PROF. ALEJANDRO C. PALADINI"
Unidad Ejecutora - UE
artículos
Título:
Two aquaporins, multiple ways of assembly.
Autor/es:
JOZEFKOWICZ CINTIA; ALLEVA KARINA; SCOCHERA FLORENCIA
Revista:
CHANNELS
Editorial:
LANDES BIOSCIENCE
Referencias:
Lugar: Austin, Texas; Año: 2016 vol. 10 p. 438 - 439
ISSN:
1933-6950
Resumen:
Protein oligomerization is a biological relevant event that may provide functional advantages to biological systems. The association of aquaporin (AQP) protomers to form hetero-oligomeric assemblies is a current challenging area of research. PIP1 and PIP2, members of the plant AQP subfamily named PIP (for plant plasma membrane intrinsic proteins), have been intensively studied in the recent years particularly due to their ability to hetero-oligomerize. We investigated the full characterization of the biological and biophysical properties of the different hetero-oligomeric configurations formed by red beet PIP1 and PIP2 subunits. Our results showed that PIP1 and PIP2 protomers have the ability to assemble with multiple stoichiometries, giving rise to 3:1, 1:3 or 2:2 heterotetramers, and all these tetramers are localized at the plasma membrane. A variable stoichiometry has also been proposed for strawberry PIPs and, recently, a similar result was confirmed for maize PIPs. In the case of red beet PIPs, we showed that although all stoichiometric assemblies can be formed, which one prevails depends on PIP1 and PIP2 relative expression. If one PIP monomer (PIP1 or PIP2) outnumbers the other, the assembly of 1:3 (or 3:1) heterotetramers is favored and even homotetramers of PIP1 or PIP2 can be the predominant species in the cell.