INVESTIGADORES
MUSCHIETTI jorge Prometeo
artículos
Título:
Oligomerization studies show that the kinase domain of the tomato pollen receptor kinase LePRK2 is necessary for interaction with LePRK1
Autor/es:
SALEM, TAMARA; BARBERINI, MARIA LAURA; WENGIER, DIEGO; DE PAZ, PABLO; CABANAS, MARIA; MUSCHIETTI, JORGE
Revista:
PLANT PHYSIOLOGY AND BIOCHEMISTRY
Editorial:
ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
Referencias:
Lugar: Paris; Año: 2012 vol. 53 p. 40 - 45
ISSN:
0981-9428
Resumen:
LePRK1 and LePRK2 are two pollen-specific receptor-like kinases from Solanum lycopersicum that are
involved in signaling during pollen-pistil communication. Previously, we showed that both proteins
interact in pollen and when expressed in yeast. We also showed that pollen tube length was regulated
by phosphorylation of specific residues in the juxtamembrane domain of LePRK2. To determine the
domains responsible for the interaction between LePRK1 and LePRK2, we constructed a series of
deletions, expressed them in yeast and determined their association by co-immunoprecipitation
assays. We show that deletions containing extracellular domains of LePRK1 and LePRK2 were glycosylated
in yeast and were sufficient for interaction with the corresponding full-length receptor. The
juxtamembrane domain of LePRK1 was sufficient for its interaction with LePRK2, whereas LePRK2
required its kinase domain for interaction with LePRK1. These findings suggest a role for the juxtamembrane
domain of LePRK2 in mediating intracellular dimerization and thus receptor kinase
phosphorylation.