Cortical microtubule arrays are critical in determining the growth axis of diffusely growing plant cells, and various environmental and physiological factors are known to affect the array organization. Microtubule organization is partly disrupted in the spiral1 mutant of Arabidopsis thaliana, which displays a right-handed helical growth phenotype in rapidly elongating epidermal cells. We show here that mutations in the plasma membrane Na(+)/H(+) antiporter SOS1 and its regulatory kinase SOS2 efficiently suppressed both microtubule disruption and helical growth phenotypes of spiral1, and that sos1 and sos2 roots in the absence of salt stress exhibited altered helical growth response to microtubule-interacting drugs at low doses. Salt stress also altered root growth response to the drugs in wild-type roots. Suppression of helical growth appeared to be specific to spiral1 since other helical growth mutants were not rescued. The effects of sos1 in suppressing spiral1 defects and in causing abnormal drug responses were nullified in the presence of the hkt1 Na(+) influx carrier mutation in roots but not in hypocotyls. These results suggest that cytoplasmic salt imbalance caused by insufficient SOS1 activity compromises cortical microtubule functions in which microtubule-localized SPIRAL1 is specifically involved.
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Biochem Biophys Res Commun
January 2025
State Key Laboratory of Systems Medicine for Cancer, Shanghai Cancer Institute, Renji Hospital, School of Medicine, Shanghai Jiao Tong University, Shanghai, 200032, China; Department of Gastrointestinal Surgery, Renji Hospital, School of Medicine, Shanghai Jiao Tong University, Shanghai, 200127, China. Electronic address:
PIK3CA, which encodes protein p110α, is one of the most frequently mutated oncogenes and a promising drug-target for human cancer. Previously, we demonstrate that p85β is released from PI3K complex which contain PIK3CA helical domain mutations and translocates into nucleus to regulate tri-methylation of H3K27, thereby promoting tumorigenicity. Here, we identify DIRAS2 and SOWAHB as target genes of nuclear p85β in PIK3CA-helical-domain-mutant tumors.
View Article and Find Full Text PDFPlant Direct
January 2025
Provincial Key Laboratory of Conservation and Utilization of Traditional Chinese Medicine Resources, Institute of Chinese Herbal Medicines Henan Academy of Agricultural Sciences Zhengzhou China.
The superfamily represents a class of transcription factors involved in plant growth, development, and stress responses. ., also known as safflower, is an important plant whose flowers contain carthamin, an expensive aromatic pigment with various medicinal and flavoring properties.
View Article and Find Full Text PDFEndocrinology
January 2025
Thyroid Research Unit, Department of Medicine, Icahn School of Medicine at Mount Sinai, New York, New York.
The pathogenesis of Thyroid Eye Disease (TED) has been suggested as due to signal enhancement in orbital fibroblasts as a result of autoantibody-induced, synergistic, interaction between the TSH receptor (TSHR) and the IGF-1 receptor (IGF-1R). This interaction has been explained by a "receptor cross talk", mediated via β-arrestin binding. Here, we have examined if this interaction can be mediated via direct receptor contact using modeling and experimental approaches.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
January 2025
Department of Molecular & Cellular Biosciences, University of Cincinnati, Cincinnati, OH 45267.
TGFβ family ligands are synthesized as precursors consisting of an N-terminal prodomain and C-terminal growth factor (GF) signaling domain. After proteolytic processing, the prodomain typically remains noncovalently associated with the GF, sometimes forming a high-affinity latent procomplex that requires activation. For the TGFβ family ligand anti-Müllerian hormone (AMH), the prodomain maintains a high-affinity interaction with its GF that does not render it latent.
View Article and Find Full Text PDFOncol Lett
March 2025
Pathology Department, Qinghai University Affiliated Hospital, Xining, Qinghai 810001, P.R. China.
The human cytochrome b561 (hCytb561) family consists of electron transfer transmembrane proteins characterized by six conserved α-helical transmembrane domains and two β-type heme cofactors. These proteins contribute to the regulation of iron metabolism and numerous different physiological and pathological processes by recycling ascorbic acid and maintaining iron reductase activity. Key members of this family include cytochrome b561 (CYB561), duodenal CYB561 (Dcytb), lysosomal CYB561 (LCytb), stromal cell-derived receptor 2 (SDR2) and 101F6, which are widely expressed in human tissues and participate in the pathogenesis of several diseases and tumors.
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