Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structural and functional analysis of SoPIP2;1 mutants adds insight into plant aquaporin gating.

Journal of molecular biology - 3 Apr 2009

Nyblom Maria, Frick Anna, Wang Yi, Ekvall Mikael, Hallgren Karin, Hedfalk Kristina, Neutze Richard, Tajkhorshid Emad, Törnroth-Horsefield Susanna

Abstract excerpt

Plant plasma membrane aquaporins facilitate water flux into and out of plant cells, thus coupling their cellular function to basic aspects of plant physiology. Posttranslational modifications of conserved phosphorylation sites, changes in cytoplasmic pH and the binding of Ca(2+) can regulate water transport activity by gating the plasma membrane aquaporins. A structural mechanism unifying these diverse...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Aquaporins
Share to Cell Membrane Permeability

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Crystallization

Share to Serine

Share to Spinacia oleracea

Share to Static Electricity

Share to X-Ray Diffraction

Source

Identifiers

PMID: 19302796
DOI: 10.1016/j.jmb.2009.01.065

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural and functional analysis of SoPIP2;1 mutants adds insight into plant aquaporin gating.PMID 19302796Read ↗

To gate or not to gate: using molecular dynamics simulations to morph gated plant aquaporins into constitutively open conformations.Semantic proximity Read ↗

Structural basis for pH gating of plant aquaporins.Semantic proximity Read ↗

The Camelina aquaporin CsPIP2;1 is regulated by phosphorylation at Ser273, but not at Ser277, of the C-terminus and is involved in salt- and drought-stress responses.Semantic proximity Read ↗

A disease mutation reveals a non-swapped pore and rewired gating cycle of the mechanically activated PIEZO1 channelSemantic proximity Read ↗

Single Mutations in the Transmembrane Domains of Maize Plasma Membrane Aquaporins Affect the Activity of Monomers within a Heterotetramer.Semantic proximity Read ↗

Loop B serine of a plasma membrane aquaporin type PIP2 but not PIP1 plays a key role in pH sensing.Semantic proximity Read ↗

Structure and Function of TPC1 Vacuole SV Channel Gains Shape.Semantic proximity Read ↗

Aquaporins Contribute to ABA-Triggered Stomatal Closure through OST1-Mediated Phosphorylation.Semantic proximity Read ↗

Mechanistic insights into phosphoactivation of SLAC1 in guard cell signaling.Semantic proximity Read ↗

On the pH regulation of plant aquaporins.Semantic proximity Read ↗

Identification of a residue in helix 2 of rice plasma membrane intrinsic proteins that influences water permeability.Semantic proximity Read ↗

Gating of the two-pore cation channel AtTPC1 in the plant vacuole is based on a single voltage-sensing domain.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.