SCF E3 LIGASE REDOX REGULATION: IMPACT ON HORMONAL SIGNALINGS

IGLESIAS, M. J.; TERRILE, M. C.; CASALONGUE, C.A.

Córdoba. Argentina

Congreso; 52th Annual Meeting Argentine Society for Biochemistry and Molecular Biology; 2016

SAIB

In plants, the ubiquitin-proteasome system action has been associated to the regulation of hormone biosynthesis, transport andperception providing a direct mechanism to modulate intensity and duration of different hormonal signalings. Ubiquitin is covalentlyattached to substrate proteins through the action of a sequential cascade of three enzymes consisting of E1, E2, and E3. The SCFcomplex is the best characterized multi-subunit ubiquitin E3 ligase. In SCF complex, SKP1 acts as a bridge between CUL1 and the Fboxproteins that mediate substrate recruitment. F-box are able to associate with SKP1 in an interchangeable manner to form diverseSCF complexes with different substrate specificities. Several phytohormone receptors are F-box proteins in SCF complexes regulatingauxin, jasmonates and gibberellins signalings.