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Shin, J. M.

Publications and source records attributed to Shin, J. M..

2 recordsLinked to original sources

F-actin regulates polarized secretion of pollen tube attractants in Arabidopsis synergid cell.

Pollen tube attraction is a key event of sexual reproduction in flowering plants. In the ovule, two synergid cells neighboring the egg cell control pollen tube arrival via the active secretion of attractant peptides such as AtLURE1 and XIUQIU from the filiform apparatus facing toward the micropyle. Distinctive cell polarity together with longitudinal F-actin and microtubules are hallmarks of the synergid cell in various species, though functions of these cellular structures are still unclear. In this study we used genetic and pharmacological approaches to elucidate the roles of cytoskeletal components in filiform apparatus formation and pollen tube guidance in Arabidopsis thaliana. Inhibition of microtubule formation reduced invaginations of the plasma membrane but did not abolish micropylar AtLURE1.2 accumulation. In contrast, the expression of a dominant-negative form of ACTIN8 induced disorganization of the filiform apparatus and loss of polar AtLURE1.2 distribution toward the filiform apparatus. Interestingly, after pollen tube reception, F-actin became unclear for a few hours in the persistent synergid cell, which may be involved in pausing and resuming pollen tube attraction during early polytubey block. Our data propose the central role of F-actin in the maintenance of cell polarity and function of male-female communication in the synergid cell.

plant biology↗

Peroxiredoxin-mediated HMGB1 oxidation and secretion in response to inflammatory stimuli

The nuclear protein HMGB1 (high mobility group box 1) is secreted by monocytesmacrophages in response to inflammatory stimuli and serves as a danger-associated molecular pattern. Acetylation and phosphorylation of HMGB1 are implicated in the regulation of its nucleocytoplasmic translocation for secretion, although inflammatory stimuli are also known to induce H2O2 production. Here we show that H2O2-induced oxidation of HMGB1 that results in formation of an intramolecular disulphide bond between Cys23 and Cys45 is necessary and sufficient for its nucleocytoplasmic translocation and secretion. The oxidation is catalysed by peroxiredoxin I (PrxI) and PrxII, which are first oxidized by H2O2 and then transfer their disulphide oxidation state to HMGB1. The disulphide form of HMGB1 showed a higher affinity for the nuclear exportin CRM1 compared with the reduced form. Lipopolysaccharide (LPS)-induced HMGB1 secretion was greatly attenuated in macrophages derived from PrxI or PrxII knockout mice, as was the LPS-induced increase in serum HMGB1 levels in these mice.

immunology↗