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COLD6-OSM1 module senses chilling for the tolerance via 2',3'-cAMP signal in rice

ABSTRACT: To further elucidate how COLD6 regulates rice chilling tolerance, we investigated COLD6 interacting proteins using COLD6ind-GFP transgenic line by immunoprecipitation in combination with mass spectrometry (IP-MS). COLD6ind-GFP was applied to bind proteins in chilling-treated rice seedling samples, and the proteins bound at the plasma membrane were subsequently extracted for further analysis. We identified 44 potential interacted proteins with COLD6.Osmotin-like protein (OSM1, LOC_Os12g38170), known for its involvement in plant abiotic stress, was found in two independent experiments.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Oryza Sativa (rice)

TISSUE(S): Plant Cell, Whole Body

SUBMITTER: 伟罗

LAB HEAD: Wei Luo

PROVIDER: PXD049115 | Pride | 2024-11-02

REPOSITORIES: Pride

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Publications

COLD6-OSM1 module senses chilling for cold tolerance via 2',3'-cAMP signaling in rice.

Luo Wei W Xu Yunyuan Y Cao Jie J Guo Xiaoyu X Han Jingdan J Zhang Yuanyuan Y Niu Yuda Y Zhang Meiling M Wang Yi Y Liang Guohua G Qian Qian Q Ge Song S Chong Kang K

Molecular cell 20241030 21

While it is known that temperature sensors trigger calcium (Ca<sup>2+</sup>) signaling to confer cold tolerance in cells, less is known about sensors that couple with other secondary messengers. Here, we identify a cold sensor complex of CHILLING-TOLERANCE DIVERGENCE 6 (COLD6) and osmotin-like 1 (OSM1), which triggers 2',3'-cyclic adenosine monophosphate (2',3'-cAMP) production to enhance cold tolerance in rice. COLD6, which is encoded by a major quantitative trait locus (QTL) gene, interacts wi ...[more]

PMID: 39481382

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COLD6-OSM1 module senses chilling for the tolerance via 2',3'-cAMP signal in rice

Project description:To further elucidate how COLD6 regulates rice chilling tolerance, we investigated COLD6 interacting proteins using COLD6ind-GFP transgenic line by immunoprecipitation in combination with mass spectrometry (IP-MS). COLD6ind-GFP was applied to bind proteins in chilling-treated rice seedling samples, and the proteins bound at the plasma membrane were subsequently extracted for further analysis. We identified 44 potential interacted proteins with COLD6. Osmotin-like protein (OSM1, LOC_Os12g38170), known for its involvement in plant abiotic stress, was found in two independent experiments.

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NLRP6 controls PTEN stability by promoting autophagic degradation of p85α to drive tumorigenesis

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2023-07-02 | PXD037436 | Pride

Deubiquitinase JOSD2 promotes non-small cell lung cancer proliferation via deubiquitylation and inactivation of LKB1

Project description:Deubiquitinases (DUBs), frequently overactivated in cancers, are associated with tumorigenesis and regarded as promising therapeutic targets. However, the underlying mechanism of DUBs promoting non-small cell lung cancer (NSCLC) are poorly understood. Through a global analysis of the contribution of 97 DUBs in NSCLC survival possibilities by The Cancer Genome Atlas (TCGA) database, we found that high expression of Josephin Domain-containing protein 2 (JOSD2) predicted the poor prognosis of patients. Depletion of JOSD2 significantly impeded NSCLC growth in vivo in both cell/patient-derived xenografts. Mechanistically, JOSD2 inhibits LKB1 kinase activity by removing K6-linked polyubiquitination, which was critical for maintaining LKB1-STRAD-MO25 complex integrity. Furthermore, we identified the first small molecule inhibitor of JOSD2 and the pharmacological inhibition of JOSD2 significantly arrested NSCLC proliferation in vitro/in vivo. Notably, our findings demonstrate a crucial role of JOSD2 in hindering LKB1 activity, highlighting JOSD2 as a potential therapeutic target in NSCLC and providing its inhibitors as a promising strategy for NSCLC treatment.

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Pharmacological Targeting of Casein Kinase 1δ Suppresses Oncogenic NRAS-Driven Melanoma

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Cyclipostins and Cyclophostin analogs impair growth of Mycobacterium abscessus by inhibiting enzymes involved in many physiological processes

Project description:Mycobacterium abscessus is nowadays under the spotlight of the scientific community. This pathogenic mycobacteria is indeed responsible for a wide spectrum of infections involving mostly pulmonary infections in patients with cystic fibrosis. M. abscessus is intrinsically resistant to a broad range of antibiotics, including most antitubercular drugs, and is considered the most pathogenic and chemotherapy-resistant rapidly growing mycobacterium. Consequently, with very limited treatment options, the development of new therapeutic approaches to fight this pathogen are urgently needed. 38 new analogs of Cyclipostins & Cyclophostin (CyC), compounds naturally produced by Streptomyces species, have been synthesized. Their antibacterial activities against clinical isolates belonging to the M. chelonae-abscessus clade, as well as Gram-negative and Gram-positive bacteria have been evaluated by the REMA method. The intracellular activities of the CyC against intramacrophagic M. abscessus have also been investigated and compared to those of imipenem. The CyCs displayed very low toxicity towards host cells and their inhibitory activity was exclusively restricted to mycobacteria. The best candidate, CyC17, showed a high selectivity for mycobacteria with MIC values (<2 up to 40 µg/mL) comparable to those of most classical antibiotics used to treat M. abscessus infections. Of importance, several CyCs were active against extracellular M. abscessus growth (i.e., CyC17 / CyC18β / CyC25 / CyC26) or against intracellular mycobacteria inside macrophages (i.e., CyC7α,β / CyC8α,β) with MIC values similar to or better than those of standard antibiotics. Based on these results, we intended to identify the potential target enzymes of CyC17/CyC26 in M. abscessus by activity-based protein profiling (ABPP) approach coupled with mass spectrometry differential analysis.

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