6533b85cfe1ef96bd12bc0e1
RESEARCH PRODUCT
ß-COP mutants show specific high sensitivity to chloride ions.
María Jesús MarcoteCésar Bernat-silvestreFernando AnientoJudit Sánchez-simarrosubject
0106 biological sciences0301 basic medicineShort CommunicationMutantArabidopsisSalt (chemistry)Plant ScienceBiology01 natural sciencesChlorideCoatomer Protein03 medical and health sciencessymbols.namesakeChloridesArabidopsismedicinechemistry.chemical_classificationIonsVesicleCOPIGolgi apparatusbiology.organism_classificationhumanitiesProtein Subunits030104 developmental biologyPhenotypechemistryCoatomerMutationsymbolsBiophysics010606 plant biology & botanymedicine.drugProtein Bindingdescription
Coat Protein I (COPI) consists of a complex (coatomer) formed by seven subunits (α-, β-, β’-, γ-, δ-, ε-, and ζ-COP) that is recruited to Golgi membranes to form vesicles that shuttle from the Golgi apparatus to the ER and between Golgi stacks. Recently, it has been described that loss of function mutants of the two Arabidopsis β-COP genes, β1-COP and β2-COP, showed increased sensitivity to salt stress (NaCl). Using a mixture of either Na(+) or Cl(−) salts, we have now found that β-COP mutants are specifically and highly sensitive to chloride ions.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2021-01-13 | Plant signalingbehavior |