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

Diacidic motif is required for efficient transport of the K+ channel KAT1 to the plasma membrane.

Plant physiology - 1 Nov 2006

Mikosch Melanie, Hurst Annette C, Hertel Brigitte, Homann Ulrike

Abstract excerpt

For a number of mammalian ion channels, trafficking to the plasma membrane was found to be controlled by intrinsic sequence motifs. Among these sequences are diacidic motifs that function as endoplasmic reticulum (ER) export signals. So far it is unclear if similar motifs also exist in plant ion...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Motifs
Share to Arabidopsis Proteins
Share to Cell Line

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cell Membrane

Share to Endoplasmic Reticulum

Share to Molecular Sequence Data

Share to Potassium Channels, Inwardly Rectifying

Share to Protein Transport

Source

Open in PubMed Open full text

Identifiers

PMID: 16950859
DOI: 10.1104/pp.106.087064
PMCID: PMC1630742

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-16950859-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Diacidic motif is required for efficient transport of the K+ channel KAT1 to the plasma membrane.PMID 16950859Read ↗

ER export of KAT1 is correlated to the number of acidic residues within a triacidic motif.Semantic proximity Read ↗

Targeting of vacuolar membrane localized members of the TPK channel family.Semantic proximity Read ↗

Endoplasmic reticulum export of glycosyltransferases depends on interaction of a cytoplasmic dibasic motif with Sar1.Semantic proximity Read ↗

Three distinct motifs within the C-terminus of acid-sensing ion channel 1a regulate its surface trafficking.Semantic proximity Read ↗

Trans-Golgi network-located AP1 gamma adaptins mediate dileucine motif-directed vacuolar targeting in Arabidopsis.Semantic proximity Read ↗

The Prenylated Rab GTPase Receptor PRA1.F4 Contributes to Protein Exit from the Golgi Apparatus.Semantic proximity Read ↗

The Arabidopsis V-ATPase is localized to the TGN/EE via a seed plant-specific motif.Semantic proximity Read ↗

ARABIDOPSIS CRINKLY4 function, internalization, and turnover are dependent on the extracellular crinkly repeat domain.Semantic proximity Read ↗

The intracellular distal tail of the Na+/H+ exchanger NHE1 is intrinsically disordered: implications for NHE1 trafficking.Semantic proximity Read ↗

Distinct roles of the last transmembrane domain in controlling Arabidopsis K+ channel activity.Semantic proximity Read ↗

Trafficking of plant vacuolar invertases: from a membrane-anchored to a soluble status. Understanding sorting information in their complex N-terminal motifs.Semantic proximity Read ↗

The potassium channel KAT1 is activated by plant and animal 14-3-3 proteins.Semantic proximity Read ↗

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