BAIT

PIN1

ARABIDOPSIS THALIANA PIN-FORMED 1, ATPIN1, F6D5.2, F6D5_2, PIN-FORMED 1, AT1G73590
auxin efflux carrier component 1
Arabidopsis thaliana (Columbia)
PREY

RCN1

ATB BETA BETA, EER1, ENHANCED ETHYLENE RESPONSE 1, F2J7.19, F2J7_19, PHOSPHOPROTEIN PHOSPHATASE 2A REGULATORY SUBUNIT A, REGA, ROOTS CURL IN NPA, SERINE/THREONINE PROTEIN PHOSPHATASE TYPE 2A REGULATORY SUBUNIT A, AT1G25490
serine/threonine-protein phosphatase 2A regulatory subunit A alpha isoform
Arabidopsis thaliana (Columbia)

PCA

A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay.

Publication

A PP6-Type Phosphatase Holoenzyme Directly Regulates PIN Phosphorylation and Auxin Efflux in Arabidopsis.

Dai M, Zhang C, Kania U, Chen F, Xue Q, McCray T, Li G, Qin G, Wakeley M, Terzaghi W, Wan J, Zhao Y, Xu J, Friml J, Deng XW, Wang H

The directional transport of the phytohormone auxin depends on the phosphorylation status and polar localization of PIN-FORMED (PIN) auxin efflux proteins. While PINIOD (PID) kinase is directly involved in the phosphorylation of PIN proteins, the phosphatase holoenzyme complexes that dephosphorylate PIN proteins remain elusive. Here, we demonstrate that mutations simultaneously disrupting the function of Arabidopsis thaliana FyPP1 (for Phytochrome-associated serine/threonine ... [more]

Unknown Jun. 21, 2012; 0(0); [Pubmed: 22715043]

Throughput

  • Low Throughput

Curated By

  • BioGRID