Pascal Genschik, PhD. Group leader at UPR 2357 – IBMP CNRS
![Genschik Pascal](https://labex-netrna.cnrs.fr/wp-content/uploads/2021/05/Genschik_Pascal.jpg)
Contact
Pascal Genschik
Phone
E-Mail
Website
UPR 2357 – IBMP CNRS
Institut de Biologie Moléculaire des Plantes du CNRS
12 rue du Général Zimmer
67084 Strasbourg Cedex
France
Research topics
- Protein degradation pathways in the model plant Arabidopsis thaliana
- Role of Cullin-RING E3 ubiquitin Ligases in plant development and stress responses
- Post-translational regulations of the RNA silencing machinery
Role in NetRNA
The group of Pascal Genschik will investigate post-translational regulations that control RNA silencing in the model plant Arabidopsis thaliana. In particular, our group should provide insights into regulatory mechanisms that control and mediate RISC (RNA induced silencing complex) turnover in normal and stress conditions.
Working Group
Publications
2020
Skiljaica, A; Lechner, E; Jagic, M; Majsec, K; Malenica, N; Genschik, P; Bauer, N
The protein turnover of Arabidopsis BPM1 is involved in regulation of flowering time and abiotic stress response Article de journal
Dans: Plant Mol Biol, vol. 102, no. 4-5, p. 359-372, 2020, ISBN: 31848919, (1573-5028 (Electronic) 0167-4412 (Linking) Journal Article).
@article{nokey,
title = {The protein turnover of Arabidopsis BPM1 is involved in regulation of flowering time and abiotic stress response},
author = {A Skiljaica and E Lechner and M Jagic and K Majsec and N Malenica and P Genschik and N Bauer},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=31848919},
doi = {10.1007/s11103-019-00947-2},
isbn = {31848919},
year = {2020},
date = {2020-01-01},
journal = {Plant Mol Biol},
volume = {102},
number = {4-5},
pages = {359-372},
abstract = {KEY MESSAGE: Protein degradation is essential in plant growth and development. The stability of Cullin3 substrate adaptor protein BPM1 is regulated by multiple environmental cues pointing on manifold control of targeted protein degradation. A small family of six MATH-BTB genes (BPM1-6) is described in Arabidopsis thaliana. BPM proteins are part of the Cullin E3 ubiquitin ligase complexes and are known to bind at least three families of transcription factors: ERF/AP2 class I, homeobox-leucine zipper and R2R3 MYB. By targeting these transcription factors for ubiquitination and subsequent proteasomal degradation, BPMs play an important role in plant flowering, seed development and abiotic stress response. In this study, we generated BPM1-overexpressing plants that showed an early flowering phenotype, resistance to abscisic acid and tolerance to osmotic stress. We analyzed BPM1-GFP protein stability and found that the protein has a high turnover rate and is degraded by the proteasome 26S in a Cullin-dependent manner. Finally, we found that BPM1 protein stability is environmentally conditioned. Darkness and salt stress triggered BPM1 degradation, whereas elevated temperature enhanced BPM1 stability and accumulation in planta.},
note = {1573-5028 (Electronic)
0167-4412 (Linking)
Journal Article},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Chico, J M; Lechner, E; Fernandez-Barbero, G; Canibano, E; Garcia-Casado, G; Franco-Zorrilla, J M; Hammann, P; Zamarreno, A M; Garcia-Mina, J M; Rubio, V; Genschik, P; Solano, R
CUL3(BPM) E3 ubiquitin ligases regulate MYC2, MYC3, and MYC4 stability and JA responses Article de journal
Dans: Proc Natl Acad Sci U S A, vol. 117, no. 11, p. 6205-6215, 2020, ISBN: 32123086, (1091-6490 (Electronic) 0027-8424 (Linking) Journal Article Research Support, Non-U.S. Gov't).
@article{nokey,
title = {CUL3(BPM) E3 ubiquitin ligases regulate MYC2, MYC3, and MYC4 stability and JA responses},
author = {J M Chico and E Lechner and G Fernandez-Barbero and E Canibano and G Garcia-Casado and J M Franco-Zorrilla and P Hammann and A M Zamarreno and J M Garcia-Mina and V Rubio and P Genschik and R Solano},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=32123086},
doi = {10.1073/pnas.1912199117},
isbn = {32123086},
year = {2020},
date = {2020-01-01},
journal = {Proc Natl Acad Sci U S A},
volume = {117},
number = {11},
pages = {6205-6215},
abstract = {The jasmonate (JA)-pathway regulators MYC2, MYC3, and MYC4 are central nodes in plant signaling networks integrating environmental and developmental signals to fine-tune JA defenses and plant growth. Continuous activation of MYC activity is potentially lethal. Hence, MYCs need to be tightly regulated in order to optimize plant fitness. Among the increasing number of mechanisms regulating MYC activity, protein stability is arising as a major player. However, how the levels of MYC proteins are modulated is still poorly understood. Here, we report that MYC2, MYC3, and MYC4 are targets of BPM (BTB/POZ-MATH) proteins, which act as substrate adaptors of CUL3-based E3 ubiquitin ligases. Reduction of function of CUL3(BPM) in amiR-bpm lines, bpm235 triple mutants, and cul3ab double mutants enhances MYC2 and MYC3 stability and accumulation and potentiates plant responses to JA such as root-growth inhibition and MYC-regulated gene expression. Moreover, MYC3 polyubiquitination levels are reduced in amiR-bpm lines. BPM3 protein is stabilized by JA, suggesting a negative feedback regulatory mechanism to control MYC activity, avoiding harmful runaway responses. Our results uncover a layer for JA-pathway regulation by CUL3(BPM)-mediated degradation of MYC transcription factors.},
note = {1091-6490 (Electronic)
0027-8424 (Linking)
Journal Article
Research Support, Non-U.S. Gov't},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
2019
Trolet, A; Baldrich, P; Criqui, M C; Dubois, M; Clavel, M; Meyers, B C; Genschik, P
Cell Cycle-Dependent Regulation and Function of ARGONAUTE1 in Plants Article de journal
Dans: Plant Cell, vol. 31, no. 8, p. 1734-1750, 2019, ISBN: 31189739, (1532-298X (Electronic) 1040-4651 (Linking) Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.).
@article{nokey,
title = {Cell Cycle-Dependent Regulation and Function of ARGONAUTE1 in Plants},
author = {A Trolet and P Baldrich and M C Criqui and M Dubois and M Clavel and B C Meyers and P Genschik},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=31189739},
doi = {10.1105/tpc.19.00069},
isbn = {31189739},
year = {2019},
date = {2019-01-01},
journal = {Plant Cell},
volume = {31},
number = {8},
pages = {1734-1750},
abstract = {Regulated gene expression is key to the orchestrated progression of the cell cycle. Many genes are expressed at specific points in the cell cycle, including important cell cycle regulators, plus factors involved in signal transduction, hormonal regulation, and metabolic control. We demonstrate that post-embryonic depletion of Arabidopsis (Arabidopsis thaliana) ARGONAUTE1 (AGO1), the main effector of plant microRNAs (miRNAs), impairs cell division in the root meristem. We utilized the highly synchronizable tobacco (Nicotiana tabacum) Bright yellow 2 (BY2) cell suspension to analyze mRNA, small RNAs, and mRNA cleavage products of synchronized BY2 cells at S, G2, M, and G1 phases of the cell cycle. This revealed that in plants, only a few miRNAs show differential accumulation during the cell cycle, and miRNA-target pairs were only identified for a small proportion of the more than 13,000 differentially expressed genes during the cell cycle. However, this unique set of miRNA-target pairs could be key to attenuate the expression of several transcription factors and disease resistance genes. We also demonstrate that AGO1 binds to a set of 19-nucleotide, tRNA-derived fragments during the cell cycle progression.},
note = {1532-298X (Electronic)
1040-4651 (Linking)
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Michaeli, S; Clavel, M; Lechner, E; Viotti, C; Wu, J; Dubois, M; Hacquard, T; Derrien, B; Izquierdo, E; Lecorbeiller, M; Bouteiller, N; Cilia, J De; Ziegler-Graff, V; Vaucheret, H; Galili, G; Genschik, P
The viral F-box protein P0 induces an ER-derived autophagy degradation pathway for the clearance of membrane-bound AGO1 Article de journal
Dans: Proc Natl Acad Sci U S A, vol. 116, no. 45, p. 22872-22883, 2019, ISBN: 31628252, (1091-6490 (Electronic) 0027-8424 (Linking) Journal Article).
@article{nokey,
title = {The viral F-box protein P0 induces an ER-derived autophagy degradation pathway for the clearance of membrane-bound AGO1},
author = {S Michaeli and M Clavel and E Lechner and C Viotti and J Wu and M Dubois and T Hacquard and B Derrien and E Izquierdo and M Lecorbeiller and N Bouteiller and J De Cilia and V Ziegler-Graff and H Vaucheret and G Galili and P Genschik},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=31628252},
doi = {10.1073/pnas.1912222116},
isbn = {31628252},
year = {2019},
date = {2019-01-01},
journal = {Proc Natl Acad Sci U S A},
volume = {116},
number = {45},
pages = {22872-22883},
abstract = {RNA silencing is a major antiviral defense mechanism in plants and invertebrates. Plant ARGONAUTE1 (AGO1) is pivotal in RNA silencing, and hence is a major target for counteracting viral suppressors of RNA-silencing proteins (VSRs). P0 from Turnip yellows virus (TuYV) is a VSR that was previously shown to trigger AGO1 degradation via an autophagy-like process. However, the identity of host proteins involved and the cellular site at which AGO1 and P0 interact were unknown. Here we report that P0 and AGO1 associate on the endoplasmic reticulum (ER), resulting in their loading into ER-associated vesicles that are mobilized to the vacuole in an ATG5- and ATG7-dependent manner. We further identified ATG8-Interacting proteins 1 and 2 (ATI1 and ATI2) as proteins that associate with P0 and interact with AGO1 on the ER up to the vacuole. Notably, ATI1 and ATI2 belong to an endogenous degradation pathway of ER-associated AGO1 that is significantly induced following P0 expression. Accordingly, ATI1 and ATI2 deficiency causes a significant increase in posttranscriptional gene silencing (PTGS) activity. Collectively, we identify ATI1 and ATI2 as components of an ER-associated AGO1 turnover and proper PTGS maintenance and further show how the VSR P0 manipulates this pathway.},
note = {1091-6490 (Electronic)
0027-8424 (Linking)
Journal Article},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Julian, J; Coego, A; Lozano-Juste, J; Lechner, E; Wu, Q; Zhang, X; Merilo, E; Belda-Palazon, B; Park, S Y; Cutler, S R; An, C; Genschik, P; Rodriguez, P L
The MATH-BTB BPM3 and BPM5 subunits of Cullin3-RING E3 ubiquitin ligases target PP2CA and other clade A PP2Cs for degradation Article de journal
Dans: Proc Natl Acad Sci U S A, vol. 116, no. 31, p. 15725-15734, 2019, ISBN: 31308219, (1091-6490 (Electronic) 0027-8424 (Linking) Journal Article Research Support, Non-U.S. Gov't).
@article{nokey,
title = {The MATH-BTB BPM3 and BPM5 subunits of Cullin3-RING E3 ubiquitin ligases target PP2CA and other clade A PP2Cs for degradation},
author = {J Julian and A Coego and J Lozano-Juste and E Lechner and Q Wu and X Zhang and E Merilo and B Belda-Palazon and S Y Park and S R Cutler and C An and P Genschik and P L Rodriguez},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=31308219},
doi = {10.1073/pnas.1908677116},
isbn = {31308219},
year = {2019},
date = {2019-01-01},
journal = {Proc Natl Acad Sci U S A},
volume = {116},
number = {31},
pages = {15725-15734},
abstract = {Early abscisic acid signaling involves degradation of clade A protein phosphatases type 2C (PP2Cs) as a complementary mechanism to PYR/PYL/RCAR-mediated inhibition of PP2C activity. At later steps, ABA induces up-regulation of PP2C transcripts and protein levels as a negative feedback mechanism. Therefore, resetting of ABA signaling also requires PP2C degradation to avoid excessive ABA-induced accumulation of PP2Cs. It has been demonstrated that ABA induces the degradation of existing ABI1 and PP2CA through the PUB12/13 and RGLG1/5 E3 ligases, respectively. However, other unidentified E3 ligases are predicted to regulate protein stability of clade A PP2Cs as well. In this work, we identified BTB/POZ AND MATH DOMAIN proteins (BPMs), substrate adaptors of the multimeric cullin3 (CUL3)-RING-based E3 ligases (CRL3s), as PP2CA-interacting proteins. BPM3 and BPM5 interact in the nucleus with PP2CA as well as with ABI1, ABI2, and HAB1. BPM3 and BPM5 accelerate the turnover of PP2Cs in an ABA-dependent manner and their overexpression leads to enhanced ABA sensitivity, whereas bpm3 bpm5 plants show increased accumulation of PP2CA, ABI1 and HAB1, which leads to global diminished ABA sensitivity. Using biochemical and genetic assays, we demonstrated that ubiquitination of PP2CA depends on BPM function. Given the formation of receptor-ABA-phosphatase ternary complexes is markedly affected by the abundance of protein components and ABA concentration, we reveal that BPMs and multimeric CRL3 E3 ligases are important modulators of PP2C coreceptor levels to regulate early ABA signaling as well as the later desensitizing-resetting steps.},
note = {1091-6490 (Electronic)
0027-8424 (Linking)
Journal Article
Research Support, Non-U.S. Gov't},
keywords = {},
pubstate = {published},
tppubtype = {article}
}