Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on Enzyme Commission mapping
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic Gene Ontology annotation based on Rhea mapping
Electronic Gene Ontology annotations created by ARBA machine learning models
Regulation of auxin response by the protein kinase PINOID.
-
PID encodes an active serine/threonine protein kinase.
"PID, which encodes a serine-threonine protein kinase"
The PINOID protein kinase regulates organ development in Arabidopsis by enhancing polar auxin transport.
-
Serine/threonine kinase by sequence similarity, consistent with later direct evidence.
"The PINOID gene was recently cloned and found to encode a protein-serine/threonine kinase."
PINOID-mediated signaling involves calcium-binding proteins.
-
Physical interaction of PID with TOUCH3 (CML12), a calmodulin-related protein. GO:0005515 protein binding conveys no molecular function.
"PID interacts with two calcium-binding proteins: TOUCH3 (TCH3), a calmodulin-related protein, and PID-BINDING PROTEIN 1 (PBP1)"
Growth signalling pathways in Arabidopsis and the AGC protein kinases.
-
Kinase activity by similarity (AGC kinase review).
"The Arabidopsis AGC kinases contain sequence motives required for the docking of PDK1 and phosphorylation of their activation loop in the kinase catalytic domain."
PIN-FORMED1 and PINOID regulate boundary formation and cotyledon development in Arabidopsis embryogenesis.
-
ARBA rule for cotyledon development, reflecting pid cotyledon defects.
"the pin1 pid double mutant displays a striking phenotype that completely lacks cotyledons and bilateral symmetry"
Phosphorylation and activation of PINOID by the phospholipid signaling kinase 3-phosphoinositide-dependent protein kinase 1 (PDK1) in Arabidopsis.
-
Recombinant PID autophosphorylates and phosphorylates exogenous substrates.
"We demonstrate that intramolecular PID autophosphorylation is required for the ability of PID to phosphorylate an exogenous substrate."
PINOID positively regulates auxin efflux in Arabidopsis root hair cells and tobacco cells.
-
Based on 35S::PID shoot and root phenotypes resembling auxin-insensitive plants, the original paper proposed that PID negatively regulates auxin signaling. Subsequent work showed that PID acts on auxin transport (PIN phosphorylation/polarity, enhanced efflux), and the phenotypes are explained by altered auxin distribution rather than a role in the TIR1/AFB signaling pathway.
"we demonstrate that the protein kinase PINOID (PID) positively regulates auxin efflux"
Antagonistic regulation of PIN phosphorylation by PP2A and PINOID directs auxin flux.
-
Physical interaction of PID with PIN1, its phosphorylation substrate. The substrate relationship is captured by the kinase activity annotation. GO:0005515 protein binding conveys no molecular function.
"PP2A and PINOID both partially colocalize with PINs and act antagonistically on the phosphorylation state of their central hydrophilic loop"
NPY1, a BTB-NPH3-like protein, plays a critical role in auxin-regulated organogenesis in Arabidopsis.
NPY genes and AGC kinases define two key steps in auxin-mediated organogenesis in Arabidopsis.
-
pid pid2 wag1 wag2 quadruple mutants lack cotyledons.
"Simultaneous disruption of PID and its 3 closest homologs (PID2, WAG1, and WAG2) completely abolishes the formation of cotyledons"
PINOID kinase regulates root gravitropism through modulation of PIN2-dependent basipetal auxin transport in Arabidopsis.
PIN phosphorylation is sufficient to mediate PIN polarity and direct auxin transport.
-
Physical interaction of PID with PIN1, its phosphorylation substrate. The substrate relationship is captured by the kinase activity annotation. GO:0005515 protein binding conveys no molecular function.
"The PIN polarity and the resulting auxin flow directionality are mediated by the antagonistic actions of PINOID kinase and protein phosphatase 2A."
Extensive signal integration by the phytohormone protein network.
-
Physical interaction of PID with MKK7/BUD1 in a large-scale phytohormone interactome (Y2H). GO:0005515 protein binding conveys no molecular function.
"we experimentally generated a systems-level map of the Arabidopsis phytohormone signalling network"
AGC kinases and MAB4/MEL proteins maintain PIN polarity by limiting lateral diffusion in plant cells.
A PINOID-dependent binary switch in apical-basal PIN polar targeting directs auxin efflux.
-
NEW annotation. PID phosphorylation of PIN hydrophilic loops is the step that sorts PINs to the apical plasma membrane: PID overexpression shifts PINs basal-to-apical and pid loss shifts PIN1 apical-to-basal at the inflorescence apex. PID thus catalyses the regulatory step of PIN polar targeting that determines auxin flow direction.
"Overexpression of the PINOID protein kinase induces a basal-to-apical shift in PIN localization"
PIN auxin efflux carrier polarity is regulated by PINOID kinase-mediated recruitment into GNOM-independent trafficking in Arabidopsis.
-
AGCVIII family serine/threonine kinase activity; PID (AT2G34650) is itself an experimental donor.
"The Ser/Thr protein kinase PINOID (PID) catalyzes PIN phosphorylation and crucially contributes to the regulation of apical-basal PIN polarity."
Auxin efflux by PIN-FORMED proteins is activated by two different protein kinases, D6 PROTEIN KINASE and PINOID.
-
NEW annotation. PID (and WAG kinases) directly activate PIN-mediated auxin efflux in Xenopus oocytes, and PID overexpression enhances auxin efflux in plant cells; PID is therefore a direct regulator of polar auxin transport, in addition to setting PIN polarity.
"PIN-mediated auxin transport is directly activated by D6 PROTEIN KINASE (D6PK) and PINOID (PID)/WAG kinases of the Arabidopsis AGCVIII kinase family"
Structural and functional insights into the regulation of Arabidopsis AGC VIIIa kinases.
-
Nuclear localization remains unresolved for PID.
"preferentially localized to the cytoplasm (AGC1-7), nucleus (WAG1 and KIPK), and the cell periphery (PID)"