Reaction Mechanism of Guanosine Triphosphate Hydrolysis by the Vision-Related Protein Complex Arl3–RP2

2016 ◽  
Vol 120 (16) ◽  
pp. 3873-3879 ◽  
Author(s):  
Maria G. Khrenova ◽  
Ekaterina D. Kots ◽  
Alexander V. Nemukhin
2015 ◽  
Vol 119 (40) ◽  
pp. 12838-12845 ◽  
Author(s):  
Maria G. Khrenova ◽  
Bella L. Grigorenko ◽  
Anatoly B. Kolomeisky ◽  
Alexander V. Nemukhin

2021 ◽  
Vol 7 (33) ◽  
pp. eabi6582
Author(s):  
Tao Fu ◽  
Mingfang Zhang ◽  
Zixuan Zhou ◽  
Ping Wu ◽  
Chao Peng ◽  
...  

The recruitment of Unc-51-like kinase and TANK-binding kinase 1 complexes is essential for Nuclear dot protein 52-mediated selective autophagy and relies on the specific association of NDP52, RB1-inducible coiled-coil protein 1, and Nak-associated protein 1 (5-azacytidine-induced protein 2, AZI2). However, the underlying molecular mechanism remains elusive. Here, we find that except for the NDP52 SKIP carboxyl homology (SKICH)/RB1CC1 coiled-coil interaction, the LC3-interacting region of NDP52 can directly interact with the RB1CC1 Claw domain, as that of NAP1 FIP200-binding region (FIR). The determined crystal structures of NDP52 SKICH/RB1CC1 complex, NAP1 FIR/RB1CC1 complex, and the related NAP1 FIR/Gamma-aminobutyric acid receptor-associated protein complex not only elucidate the molecular bases underpinning the interactions of RB1CC1 with NDP52 and NAP1 but also reveal that RB1CC1 Claw and Autophagy-related protein 8 family proteins are competitive in binding to NAP1 and NDP52. Overall, our findings provide mechanistic insights into the interactions of NDP52, NAP1 with RB1CC1 and ATG8 family proteins.


2020 ◽  
Vol 6 (48) ◽  
pp. eabb7719
Author(s):  
Guojuan Xu ◽  
Xionghui Zhong ◽  
Yanlong Shi ◽  
Zhuo Liu ◽  
Nan Jiang ◽  
...  

Mitochondria are essential for animal and plant immunity. Here, we report that the effector MoCDIP4 of the fungal pathogen Magnaporthe oryzae targets the mitochondria-associated OsDjA9-OsDRP1E protein complex to reduce rice immunity. The DnaJ protein OsDjA9 interacts with the dynamin-related protein OsDRP1E and promotes the degradation of OsDRP1E, which functions in mitochondrial fission. By contrast, MoCDIP4 binds OsDjA9 to compete with OsDRP1E, resulting in OsDRP1E accumulation. Knockout of OsDjA9 or overexpression of OsDRP1E or MoCDIP4 in transgenic rice results in shortened mitochondria and enhanced susceptibility to M. oryzae. Overexpression of OsDjA9 or knockout of OsDRP1E in transgenic rice, in contrast, leads to elongated mitochondria and enhanced resistance to M. oryzae. Our study therefore reveals a previously unidentified pathogen-infection strategy in which the pathogen delivers an effector into plant cells to target an HSP40-DRP complex; the targeting leads to the perturbation of mitochondrial dynamics, thereby inhibiting mitochondria-mediated plant immunity.


2019 ◽  
Vol 105 (5) ◽  
pp. 1016-1022 ◽  
Author(s):  
Hessa S. Alsaif ◽  
Mohammad Al-Owain ◽  
Martin E. Barrios-Llerena ◽  
Ghada Gosadi ◽  
Yousef Binamer ◽  
...  

2020 ◽  
Vol 34 (S1) ◽  
pp. 1-1
Author(s):  
Loretta Jackson-Hayes ◽  
Alexis Craft ◽  
Muhammad Hameed ◽  
Zariah Hines ◽  
W. Toler Freyaldenhoven ◽  
...  

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