Dataset Information

Thermal-Enhanced bri1-301 Instability Reveals a Plasma Membrane Protein Quality Control System in Plants.

ABSTRACT: Brassinosteroids (BRs) are essential phytohormones mainly perceived by a single-pass transmembrane receptor-like protein kinase (RLK), BRASSINOSTEROID INSENSITIVE 1 (BRI1). bri1-5 and bri1-9, two distinct mutants with point mutations in the extracellular domain of BRI1, show weak defective phenotypes. Previous studies indicated that bri1-5 and bri1-9 mutated proteins can be recognized and eliminated via an endoplasmic reticulum quality control (ERQC) mechanism. Most of these two proteins, therefore, cannot reach their destination, plasma membrane. Here, we report our functional characterization of bri1-301, another BRI1 mutant protein with an amino acid substitution in the cytoplasmic kinase domain. bri1-301 is a partially functional BR receptor with significantly decreased protein abundance. Interestingly, protein stability and subcellular localization of bri1-301 are temperature-sensitive. At 22°C, an optimal temperature for indoor Arabidopsis growth, bri1-301 shows a weak defective phenotype. At a lower temperature condition such as 18°C, bri1-301 exhibits subtle morphological defects. At a higher temperature condition such as 28°C, on the other hand, bri1-301 displays an extremely severe phenotype reminiscent to that of a null bri1 mutant due to greatly increased bri1-301 internalization and degradation. Our detailed analyses suggest that bri1-301 stability is controlled by ERQC and plasma membrane quality control (PMQC) systems. Since PMQC has not been well studied in plants, bri1-301 can be used as a model mutant for future genetic dissection of this critical process.

SUBMITTER: Lv M

PROVIDER: S-EPMC6232910 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature

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Thermal-Enhanced bri1-301 Instability Reveals a Plasma Membrane Protein Quality Control System in Plants.

Lv Minghui M Li Meizhen M Chen Weiyue W Wang Yanze Y Sun Chao C Yin Hongju H He Kai K Li Jia J

Frontiers in plant science 20181106

Brassinosteroids (BRs) are essential phytohormones mainly perceived by a single-pass transmembrane receptor-like protein kinase (RLK), BRASSINOSTEROID INSENSITIVE 1 (BRI1). <i>bri1-5</i> and <i>bri1-9</i>, two distinct mutants with point mutations in the extracellular domain of BRI1, show weak defective phenotypes. Previous studies indicated that bri1-5 and bri1-9 mutated proteins can be recognized and eliminated via an endoplasmic reticulum quality control (ERQC) mechanism. Most of these two pr ...[more]

PMID: 30459799

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Project description:Analysis of transcriptome in moss Physcomitrella patens CNGCb null mutant at 25 and 34 degrees C for 30 minutes. Results provide insight into role of CNGCb in acquired thermotolerance induced by non-lethal heat treatment. Typically at dawn of a hot summer day, land plants need precise molecular thermometers to sense harmless increments in the ambient temperature to timely develop a heat-shock response (HSR) and accumulate protective heat shock proteins (Hsps), in anticipation of upcoming harmful temperatures at mid-day. Here, we found that the CNGCb gene from Physcomitrella patens and its Arabidopsis ortholog CNGC2, encode for a component of cyclic nucleotide gated Ca2+ channels acting as the primary thermosensors of land plant cells. Disruption of CNGCb or CNGC2 produced a hyper-thermosensitive phenotype, giving rise to a HSR and acquired thermotolerance at significantly milder heat-priming treatments than in wild type plants. In an aequorin-expressing moss, CNGCb loss-of-function caused altered Ca2+ signaling and a sustained Ca2+ influx. Patch clamp recordings on moss protoplasts showed the presence of three distinct thermo-responsive Ca2+-channels in wild type cells. Deletion of CNGCb led to a total absence of one, and it increased the open probability of the remaining two thermo-responsive Ca2+ channels. Thus, both in Arabidopsis and moss, CNGC2 and CNGCb are expected to form with other related CNGCs, heteromeric Ca2+ channels in the plasma membrane that respond to mild increments in the ambient temperature by triggering an optimal HSR, leading to the onset of plant acquired thermotolerance. The WT moss tissues were heat-shocked for a half an hour at 34°C and 38°C and CNGCb at 25and 34°C followed by liquid nitrogen freezing. Total RNA was isolated using RNeasy Mini Kit (QIAGEN, Hilden, Germany) and two biological replicate samples for each treatment, were extracted. An Agilent-certified microarray service lab (MOgene, LC, St. Louis, MO, USA) was used to verify the integrity of the RNA and perform the microarray experiments. Two biological replicates were performed.

Dataset Information

Thermal-Enhanced bri1-301 Instability Reveals a Plasma Membrane Protein Quality Control System in Plants.

Publications

Thermal-Enhanced bri1-301 Instability Reveals a Plasma Membrane Protein Quality Control System in Plants.

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