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

Autophosphorylation Affects Substrate-Binding Affinity of Tobacco Ca2+-Dependent Protein Kinase1.

Plant physiology - 1 Aug 2017

Ito Takeshi, Ishida Sarahmi, Oe Shota, Fukazawa Jutarou, Takahashi Yohsuke

Abstract excerpt

Protein kinases regulate diverse physiological processes. Because many kinases preserve inherent autophosphorylation capability, autophosphorylation appears to be one of the most important mechanisms for cellular signaling. However, physiological functions of autophosphorylation are still largely unknown, other than the self-activation by phosphorylation of activation loop in the catalytic domain. REPRESSION OF...

Read the complete abstract on PubMed

Topics

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

Share to 14-3-3 Proteins
Share to Gibberellins
Share to Nicotiana

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Kinases

Share to Protein Multimerization

Share to Serine

Share to Threonine

Share to Triazoles

Source

Open in PubMed Open full text

Identifiers

PMID: 28637832
DOI: 10.1104/pp.17.00515
PMCID: PMC5543960

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Autophosphorylation Affects Substrate-Binding Affinity of Tobacco Ca2+-Dependent Protein Kinase1.PMID 28637832Read ↗

Alteration of substrate specificity: the variable N-terminal domain of tobacco Ca(2+)-dependent protein kinase is important for substrate recognition.Semantic proximity Read ↗

Mutational analysis of stress-responsive peanut dual specificity protein kinase. Identification of tyrosine residues involved in regulation of protein kinase activity.Semantic proximity Read ↗

CPK28-mediated phosphorylation enhances nitrate transport activity of NRT2.1 during nitrogen deprivation.Semantic proximity Read ↗

A protein phosphatase 2C, AP2C1, interacts with and negatively regulates the function of CIPK9 under potassium-deficient conditions in Arabidopsis.Semantic proximity Read ↗

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

Two distinct families of protein kinases are required for plant growth under high external Mg2+ concentrations in Arabidopsis.Semantic proximity Read ↗

Serine/threonine/tyrosine protein kinase from Arabidopsis thaliana is dependent on serine residues for its activity.Semantic proximity Read ↗

Autophosphorylation of Arabidopsis nucleoside diphosphate kinase 2 occurs only on its active histidine residue.Semantic proximity Read ↗

Managing activity and Ca2+ dependence through mutation in the Junction of the AtCPK1 coordinates the salt tolerance in transgenic tobacco plants.Semantic proximity Read ↗

Roles of AGCVIII Kinases in the Hypocotyl Phototropism of Arabidopsis Seedlings.Semantic proximity Read ↗

Direct phosphorylation and activation of a mitogen-activated protein kinase by a calcium-dependent protein kinase in rice.Semantic proximity Read ↗

MAPK phosphatase AP2C3 induces ectopic proliferation of epidermal cells leading to stomata development in Arabidopsis.Semantic proximity Read ↗

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