The mechanisms of plant drought resistance are unclear but may involve membrane trafficking and metabolic reprogramming, including proline accumulation. Forward genetic screening using a () identified a drought hypersensitive mutant with a single-amino acid substitution (P335L) in the nonphototrophic hypocotyl 3 (NPH3) domain of NPH3/root phototropism 2-like 5 (NRL5)/naked pins in Yucca 8 (NPY8). Further experiments found that NRL5 and other NPH3 domain proteins are guanosine triphosphatases (GTPases). NRL5, but not NRL5, interacted with the RABE1c and RABH1b GTPases and the soluble -ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) Vesicle-Associated Membrane Protein (VAMP)721/722. These proteins controlled NRL5 localization and connection to trafficking while also being genetically downstream of, and potentially regulated by, NRL5. These data demonstrate that NRL5-mediated restraint of proline catabolism is required for drought resistance and also reveal unexpected functions of the NPH3 domain such that the role of NPH3 domain proteins in signaling, trafficking, and cellular polarity can be critically reevaluated.
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http://dx.doi.org/10.1126/sciadv.ado5429 | DOI Listing |
Plant Cell Physiol
November 2024
Graduate School of Science and Technology, Niigata University, Niigata 950-2181, Japan.
Plants exhibit shoot growth in the direction of the light source to facilitate photosynthesis, known as positive phototropism. In Arabidopsis hypocotyl phototropism, it is thought that a gradient of the signal intensity of the blue light photoreceptor phototropin1 (phot1) between the light-irradiated and shaded sides leads to the differential growth of hypocotyls. The intensity of phot1 signal is regulated not only by the protein kinase activity of phot1 but also by the phosphorylation status of the NONPHOTOTROPIC HYPOCOTYL3 (NPH3) protein, which has a dark form and a blue light form of the phosphorylation modification.
View Article and Find Full Text PDFNew Phytol
December 2024
Institute of Plant and Microbial Biology, Academia Sinica, Taipei, 11529, Taiwan.
The nonphototrophic hypocotyl 3 (NPH3) domain is plant specific and of unknown function. It is nearly always attached to an N-terminal BTB domain and a largely unstructured C-terminal region. Recent reports revealed NPH3-domain GTPase activity and connection to intracellular trafficking, condensate formation, membrane attachment of the C-terminal region for some NPH3-domain proteins and, at the physiological level, drought-related function for at least one NPH3-domain protein.
View Article and Find Full Text PDFInt J Mol Sci
August 2024
State Key Laboratory of Subtropical Silviculture, College of Forestry and Biotechnology, Zhejiang A & F University, Hangzhou 311300, China.
The (Broad-complex, tramtrack, and bric-a-brac) gene family, characterized by a highly conserved BTB domain, is implicated in a spectrum of biological processes, encompassing growth and development, as well as stress responses. Characterization and functional studies of genes in poplar are still limited, especially regarding their response to hormones and biotic/abiotic stresses. In this study, we conducted an HMMER search in conjunction with BLASTp and identified 95 gene models in .
View Article and Find Full Text PDFSci Adv
August 2024
Institute of Plant and Microbial Biology, Academia Sinica, Taipei 11529, Taiwan.
The mechanisms of plant drought resistance are unclear but may involve membrane trafficking and metabolic reprogramming, including proline accumulation. Forward genetic screening using a () identified a drought hypersensitive mutant with a single-amino acid substitution (P335L) in the nonphototrophic hypocotyl 3 (NPH3) domain of NPH3/root phototropism 2-like 5 (NRL5)/naked pins in Yucca 8 (NPY8). Further experiments found that NRL5 and other NPH3 domain proteins are guanosine triphosphatases (GTPases).
View Article and Find Full Text PDFBioessays
February 2023
Department of the Control of Genetic Processes, Institute of Gene Biology Russian Academy of Sciences, Moscow, Russia.
Broad-complex, Tramtrack, and Bric-à-brac/poxvirus and zinc finger (BTB/POZ) is a conserved domain found in many eukaryotic proteins with diverse cellular functions. Recent studies revealed its importance in multiple developmental processes as well as in the onset and progression of oncological diseases. Most BTB domains can form multimers and selectively interact with non-BTB proteins.
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