Ubiquitin chain topology in plant cell signaling: a new facet to an evergreen story

Abstract

Ubiquitin is a peptide modifier able to form polymers of varying length and linkage as part of a powerful signaling system. Perhaps the best-known aspect of this protein's function is as the driver of targeted protein degradation through the Ubiquitin Proteasome System (UPS). Through the formation of lysine 48-linked polyubiquitin chains, it is able to direct the degradation of tagged proteins by the 26S proteasome, indirectly controlling many processes within the cell. However, recent research has indicated that ubiquitin performs a multitude of other roles within the cell beyond protein degradation. It is able to form 6 other "atypical" linkages though lysine residues at positions 6, 11, 27, 29, 33, and 63. These atypical chains perform a range of diverse functions, including the regulation of iron uptake in response to perceived deficiency, repair of double stranded breaks in the DNA, and regulation of the auxin response through the non-proteasomal degradation of auxin efflux carrier protein PIN1. This review explores the role ubiquitin chain topology plays in plant cellular function. We aim to highlight the importance of these varying functions and the future challenges to be encountered within this field.

Keywords: abiotic stress; pathogen; plants; signaling pathways; ubiquitin.

Figure 1

Alignment of HsUBE2S with AtUBC22 homologs and AtUBC7. An alignment showing the amino acid sequence similarity between the K11-chain-forming Human E2, UBE2S, the plant homologs AtUBC22, AlUBC18, Os06g0660700, and TuUBC22, and the K48-chain-forming AtUBC7. The alignment shows large areas of conservation amongst the K11-chain-forming E2s, but little in comparison with UBC7. The active site cysteine (red box) is conserved in all aligned sequences, with the surrounding residues showing very high conservation amongst the K11-chain-forming UBCs.