Post-translational regulation of miRNA pathway components, AGO1 and HYL1, in plants

TY - JOUR

T1 - Post-translational regulation of miRNA pathway components, AGO1 and HYL1, in plants

AU - Cho, Seok Keun

AU - Ryu, Moon Young

AU - Shah, Pratik

AU - Poulsen, Christian Peter

AU - Yang, Seong Wook

PY - 2016/8/1

Y1 - 2016/8/1

N2 - Post-translational modifications (PTMs) of proteins are essential to increase the functional diversity of the proteome. By adding chemical groups to proteins, or degrading entire proteins by phosphorylation, glycosylation, ubiquitination, neddylation, acetylation, lipidation, and proteolysis, the complexity of the proteome increases, and this then influences most biological processes. Although small RNAs are crucial regulatory elements for gene expression in most eukaryotes, PTMs of small RNA microprocessor and RNA silencing components have not been extensively investigated in plants. To date, several studies have shown that the proteolytic regulation of AGOs is important for host-pathogen interactions. DRB4 is regulated by the ubiquitin-proteasome system, and the degradation of HYL1 is modulated by a de-etiolation repressor, COP1, and an unknown cytoplasmic protease. Here, we discuss current findings on the PTMs of microprocessor and RNA silencing components in plants.

AB - Post-translational modifications (PTMs) of proteins are essential to increase the functional diversity of the proteome. By adding chemical groups to proteins, or degrading entire proteins by phosphorylation, glycosylation, ubiquitination, neddylation, acetylation, lipidation, and proteolysis, the complexity of the proteome increases, and this then influences most biological processes. Although small RNAs are crucial regulatory elements for gene expression in most eukaryotes, PTMs of small RNA microprocessor and RNA silencing components have not been extensively investigated in plants. To date, several studies have shown that the proteolytic regulation of AGOs is important for host-pathogen interactions. DRB4 is regulated by the ubiquitin-proteasome system, and the degradation of HYL1 is modulated by a de-etiolation repressor, COP1, and an unknown cytoplasmic protease. Here, we discuss current findings on the PTMs of microprocessor and RNA silencing components in plants.

KW - Journal Article

KW - Review

U2 - 10.14348/molcells.2016.0085

DO - 10.14348/molcells.2016.0085

M3 - Journal article

C2 - 27440184

SN - 1016-8478

VL - 39

SP - 581

EP - 586

JO - Molecules and Cells

JF - Molecules and Cells

IS - 8

ER -