TY  - JOUR
TI  - A hypothetical MEK1-MIP1-SMEK multiprotein signaling complex may function in <I>Dictyostelium</I> and mammalian cells

AU  - Sobko, Alex
T2  - The International Journal of Developmental Biology
AB  - In a previous study, we characterized Dictyostelium SUMO targeted ubiquitin ligase (StUbL) MIP1 that associates with protein kinase MEK1 and targets SUMOylated MEK1 to ubiquitination (Sobko et al., 2002). These modifications happen in response to activation of MEK1 by the chemoattractant cAMP.  Second site genetic suppressor of mek1- null phenotype (SMEK) was also identified in Dictyostelium. MEK1 and SMEK belong to the same linear pathway, in which MEK1 negatively regulates SMEK, which then negatively regulates chemotaxis and aggregation. RNF4 is mammalian homologue of MIP. RNF4 interacts with hSMEK2, the human homologue of Dictyostelium SMEK. We propose the existence of an evolutionarily conserved MEK1-SMEK signaling complex that upon MEK1 activation and SUMOylation, recruits ubiqutin ligase MIP1/RNF4, which, in turn, ubiquitinates SMEK and targets this protein for proteasomal degradation. This could be a mechanism for negative regulation of SMEK by MEK1 signaling.
PY  - 2020
DO  - 10.1387/ijdb.200140as
VL  - 64
IS  - 10-11-12
SP  - 495
EP  - 498
J2  - Int. J. Dev. Biol.
LA  - en
SN  - 0214-6282
SN  - 1696-3547
UR  - https://ijdb.ehu.eus/article/200140as
Y2  - 2024/11/21/18:06:06
ER  -