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

Rice small C2-domain proteins are phosphorylated by calcium-dependent protein kinase.

Molecules and cells - 1 May 2013

Kang Chang Ho, Moon Byeong Cheol, Park Hyeong Cheol, Koo Sung Cheol, Chi Yong Hun, Cheong Yong Hwa, Yoon Byung-Dae, Lee Sang Yeol, Kim Cha Young

Abstract excerpt

We previously reported that OsERG1 and OsERG3 encode rice small C2-domain proteins with different biochemical properties in Ca(2+)- and phospholipid-binding assays. Os-ERG1 exhibited Ca(2+)-dependent phospholipid binding, which was not observed with OsERG3. In the present study, we show that both OsERG1 and OsERG3 proteins exhibit oligomerization properties as determined by native polyacrylamide gel...

Read the complete abstract on PubMed

Topics

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

Share to Alanine
Share to Calcium
Share to Cell Membrane

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cytosol

Share to Phospholipids

Share to Protein Kinases

Share to Serine

Source

Open in PubMed Open full text

Identifiers

PMID: 23456295
DOI: 10.1007/s10059-013-2185-0
PMCID: PMC3887858

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Rice small C2-domain proteins are phosphorylated by calcium-dependent protein kinase.PMID 23456295Read ↗

Transcriptional activation and phosphorylation of OsCNGC9 confer enhanced chilling tolerance in rice.Semantic proximity Read ↗

Loss of calcium-dependent protein kinases OsCPK5 and OsCPK13 leads to NLR-dependent resistance in rice.Semantic proximity Read ↗

Targeted gene disruption of OsCERK1 reveals its indispensable role in chitin perception and involvement in the peptidoglycan response and immunity in rice.Semantic proximity Read ↗

A novel C2-domain phospholipid-binding protein, OsPBP1, is required for pollen fertility in rice.Semantic proximity Read ↗

Mutation of the OsSAC1 Gene, which Encodes an Endoplasmic Reticulum Protein with an Unknown Function, Causes Sugar Accumulation in Rice Leaves.Semantic proximity Read ↗

OsCYCP1;1, a PHO80 homologous protein, negatively regulates phosphate starvation signaling in the roots of rice (Oryza sativa L.).Semantic proximity Read ↗

Membrane localization of a rice calcium-dependent protein kinase (CDPK) is mediated by myristoylation and palmitoylation.Semantic proximity Read ↗

Mutation of <i>OsCDS5</i> confers broad-spectrum disease resistance in riceSemantic proximity Read ↗

Calcium signaling through protein kinases. The Arabidopsis calcium-dependent protein kinase gene family.Semantic proximity Read ↗

An S-domain receptor-like kinase, OsSIK2, confers abiotic stress tolerance and delays dark-induced leaf senescence in rice.Semantic proximity Read ↗

Characterization of the yeast tricalbins: membrane-bound multi-C2-domain proteins that form complexes involved in membrane trafficking.Semantic proximity Read ↗

Identification of a putative voltage-gated Ca2+ -permeable channel (OsTPC1) involved in Ca2+ influx and regulation of growth and development in rice.Semantic proximity Read ↗

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