Tonoplast (<i>Bv</i><scp>TIP</scp>1;2) and plasma membrane (<i>Bv</i><scp>PIP</scp>2;1) aquaporins show different mechanosensitive properties

Goldman, Ramiro Pablo; Jozefkowicz, Cintia; Fortuna, Agustina Canessa; Sutka, Moira; Alleva, Karina; Ozu, Marcelo

doi:10.1002/1873-3468.12671

Cited by 8 publications

(9 citation statements)

References 49 publications

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“…This gating mechanism would be cooperative, maybe involving the four monomers of the tetramer (Ozu et al 2013). In addition, sensitivity differences could exist between PIPs and TIPs (Goldman et al 2017). Taken together, this evidence suggests that this mechanism would have existed before divergence of PIP-AQP1like and TIP-AQP8-like AQPs.…”

Section: Gatingmentioning

confidence: 83%

“…These and other experimental evidence (Niemietz and Tyerman 1997) suggested that cell volume or pressure could be directly involved in the regulation of AQPs under hyper-and hypoosmotic conditions. Recently, mechanical gating has been probed as a possible mechanism in hAQP1 (Ozu et al 2013) and VvTIP2;1 (Leitão et al 2014), and experimentally probed for BvTIP2;1 (Goldman et al 2017). This gating mechanism would be cooperative, maybe involving the four monomers of the tetramer (Ozu et al 2013).…”

Section: Gatingmentioning

confidence: 99%

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Plant and animal aquaporins crosstalk: what can be revealed from distinct perspectives

2017

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Aquaporins (AQPs) can be revisited from a distinct and complementary perspective: the outcome from analyzing them from both plant and animal studies. (1) The approach in the study. Diversity found in both kingdoms contrasts with the limited number of crystal structures determined within each group. While the structure of almost half of mammal AQPs was resolved, only a few were resolved in plants. Strikingly, the animal structures resolved are mainly derived from the AQP2-lineage, due to their important roles in water homeostasis regulation in humans. The difference could be attributed to the approach: relevance in animal research is emphasized on pathology and in consequence drug screening that can lead to potential inhibitors, enhancers and/or regulators. By contrast, studies on plants have been mainly focused on the physiological role that AQPs play in growth, development and stress tolerance. (2) The transport capacity. Besides the well-described AQPs with high water transport capacity, large amount of evidence confirms that certain plant AQPs can carry a large list of small solutes. So far, animal AQP list is more restricted. In both kingdoms, there is a great amount of evidence on gas transport, although there is still an unsolved controversy around gas translocation as well as the role of the central pore of the tetramer. (3) More roles than expected. We found it remarkable that the view of AQPs as specific channels has evolved first toward simple transporters to molecules that can experience conformational changes triggered by biochemical and/or mechanical signals, turning them also into signaling components and/or behave as osmosensor molecules.

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Section: Gatingmentioning

confidence: 83%

Section: Gatingmentioning

confidence: 99%

Plant and animal aquaporins crosstalk: what can be revealed from distinct perspectives

2017

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“…Experimental demonstration for the tension-mediated regulation in animal and plant AQPs was reported by simultaneous measurements of mechanical coefficients and water transport rates in proteoliposomes with RnAQP4 (rat) [ 134 ] and Xenopus oocytes expressing BvTIP1;2 (beet) [ 135 ]. In both cases, the water permeability coefficient decreases in a nonlinear fashion with increments of membrane elasticity, as was predicted for AQP1 [ 38 ].…”

Section: Structural Changes That Regulate Permeationmentioning

confidence: 99%

“…As widely reported on revisions, MS ion channels activate (open) with increasing tension [ 136 , 137 , 138 , 139 ]. On the contrary, MS AQPs (AQP4, AQP1, BvTIP1;2, VvTIP2;1) decrease their water transport rate when membrane tension raises, evidencing a closure event of the water pathway [ 38 , 132 , 134 , 135 ]. However, it cannot be generalized since MD simulations performed with the structure of AQY1 from the yeast Pichia pastoris predict that this AQP would open when increasing membrane curvature [ 64 ].…”

Section: Structural Changes That Regulate Permeationmentioning

confidence: 99%

“…In analogy with the study of ion channels, the transport capacity of AQPs can be evidenced in a plot of water flux versus osmotic gradient (J w -Δ osm ). For mechanosensitive AQPs such as human AQP1 and BvTIP1;2, the J w -Δ osm plots show deviations from linearity with gradients higher than 100 mosmol·Kg w −1 [ 38 , 135 ]. This deviation shows that P f is not a constant value.…”

Section: Structural Changes That Regulate Permeationmentioning

confidence: 99%

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Aquaporins: More Than Functional Monomers in a Tetrameric Arrangement

Ozu

Galizia

Acuña

et al. 2018

Cells

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Aquaporins (AQPs) function as tetrameric structures in which each monomer has its own permeable pathway. The combination of structural biology, molecular dynamics simulations, and experimental approaches has contributed to improve our knowledge of how protein conformational changes can challenge its transport capacity, rapidly altering the membrane permeability. This review is focused on evidence that highlights the functional relationship between the monomers and the tetramer. In this sense, we address AQP permeation capacity as well as regulatory mechanisms that affect the monomer, the tetramer, or tetramers combined in complex structures. We therefore explore: (i) water permeation and recent evidence on ion permeation, including the permeation pathway controversy—each monomer versus the central pore of the tetramer—and (ii) regulatory mechanisms that cannot be attributed to independent monomers. In particular, we discuss channel gating and AQPs that sense membrane tension. For the latter we propose a possible mechanism that includes the monomer (slight changes of pore shape, the number of possible H-bonds between water molecules and pore-lining residues) and the tetramer (interactions among monomers and a positive cooperative effect).

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Membrane tension‐dependent conformational change of Isoleucine 106 of loop B diminishes water permeability in FaPIP2;1

Caviglia,

Espinoza‐Muñoz,

Alvear‐Arias

et al. 2024

Protein Science

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Aquaporins (AQPs) are membrane proteins specialized in facilitating water transport across membranes. Mechanical stress is one of the various stimuli that regulate AQPs. Briefly, there are several studies that report a decrease in permeability upon an increase in membrane tension. However, the molecular details of this mechanosensitive (MS) response are still a matter of debate. Our work attempts to close that gap in knowledge by providing evidence of a conformational change that occurs inside the pore of the strawberry aquaporin FaPIP2;1. Via osmotic shock experiments and molecular dynamics (MD) simulations, we found that a residue of loop B, I106, is key to the blocking of the permeation pathway and such a change is almost exclusively found under membrane tensile stress. In detail, osmotic shock experiments exhibited a nonlinear increment in water fluxes for increasing osmolarities, evidencing a decrease in the FaPIP2;1 permeability. MD simulations under membrane tension showed the same trend, with a significant increase in states with a low water permeability. The latter was correlated with a conformational change in I106 that generates a permeation barrier of around 18 kJ mol−1, effectively closing the pore. This work constitutes the first report of a PIP type aquaporin reacting to tensile stress in the membrane. Our findings could pave the way to test whether this conformational change is also responsible for mechanical gating in the other MS aquaporins, both those already reported and those still waiting to be found.

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Tonoplast (BvTIP1;2) and plasma membrane (BvPIP2;1) aquaporins show different mechanosensitive properties

Cited by 8 publications

References 49 publications

Plant and animal aquaporins crosstalk: what can be revealed from distinct perspectives

Plant and animal aquaporins crosstalk: what can be revealed from distinct perspectives

Aquaporins: More Than Functional Monomers in a Tetrameric Arrangement

Membrane tension‐dependent conformational change of Isoleucine 106 of loop B diminishes water permeability in FaPIP2;1

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