Type 1 protein phosphatases are very highly conserved throughout eukaryotes where they regulate a number of key metabolic and morphogenetic processes. A cDNA, AtPP1bg, representing a new member of the type 1 protein phosphatase gene family in Arabidopsis has been isolated on the basis of hybridization with the Aspergillus bimG protein phosphatase gene. The AtPP1bg gene potentially encodes a 37 kDa protein very closely related to PP1 but with divergent N- and C-termini. The predicted amino acid sequence shows 71% identity to the ORF of the bimG gene. When expressed in Aspergillus under the alcA promoter, this phosphatase complements the temperature-sensitive bimG11 mutation allowing nearly normal vegetative growth at 37 degrees C (but not at 42 degrees C). Notably, the plant PP1 does not support morphogenesis (conidiation) at 37 degrees C. This may indicate that conidophore formation has particular phosphatase requirement(s) which the plant PP1 cannot supply. The pattern of expression of the AtPP1bg transcript has been studied during development of the plant. In situ hybridization of Arabidopsis with antisense probes shows that this phosphatase gene is expressed at a low level throughout the plant, but is strongly upregulated within developing flowers, especially in the tapetum, the developing and mature pollen and in the ovaries. This implies that the AtPP1bg either has a specialized role in the formation of these organs, or that there is an increased requirement for protein phosphatase 1 at these stages. It was found that the level of AtPP1bg transcript, as judged by the relative intensity of staining in different cells within the floral meristems, did not vary during the cell cycle.
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http://dx.doi.org/10.1046/j.1365-313x.1995.07050823.x | DOI Listing |
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Guangdong Provincial Key Laboratory of Digestive Cancer Research, Digestive Diseases Center, Scientific Research Center, The Seventh Affiliated Hospital of Sun Yat-sen University, Shenzhen, Guangdong 518107, P.R. China.
CRISPR-Cas12a technology has transformative potential, but as its applications grow, enhancing its inherent functionalities is essential to meet diverse demands. Here, we reveal a regulatory mechanism for LbCas12a through direct repeat (DR) region 3' end modifications and de-modifications, which can regulate LbCas12a's cis- and trans-cleavage activities. We extensively explored the effects of introducing phosphorylation, DNA, photo-cleavable linker, DNA modifications at the DR 3' end on LbCas12a's functionality.
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School of Food Science and Technology, Dalian Polytechnic University, SKL of Marine Food Processing & Safety Control, National Engineering Research Center of Seafood, Dalian 116034, People's Republic of China.
Bone morphogenetic protein 2 (BMP-2) and a polysaccharide (SUP) were embedded in the calcium phosphate cement (CPC) scaffold, and the bone repair ability was evaluated. The new scaffolds were characterized using x-ray diffraction, Fourier transform-infrared, scanning electron microscopy, and energy dispersive spectroscopy analyses. CPC-BMP2-SUPH scaffold promoted the BMP-2 release by 1.
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Department of Pharmacology, adMare BioInnovations, Montréal, Quebec, H4S 1Z9, Canada.
The gene is nearly ubiquitously subjected to activating mutation in pancreatic adenocarcinomas (PDAC), occurring at a frequency of over 90% in tumors. Mutant KRAS drives sustained signaling through the MAPK pathway to affect frequently disrupted cancer phenotypes including transcription, proliferation and cell survival. Recent research has shown that PDAC tumor growth and survival required a guanine nucleotide exchange factor for RAS homolog family member A (RhoA) called GEF-H1.
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Key Laboratory of Plant Carbon Capture, Shanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, Shanghai 200032, China.
Plants sense and respond to hyperosmotic stress via quick activation of sucrose nonfermenting 1-related protein kinase 2 (SnRK2). Under unstressed conditions, the protein phosphatase type 2C (PP2C) in clade A interact with and inhibit SnRK2s in subgroup III, which are released from the PP2C inhibition via pyrabactin resistance 1-like (PYL) abscisic acid receptors. However, how SnRK2s are released under osmotic stress is unclear.
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Key Laboratory of Laboratory Medicine, Ministry of Education of China, School of Laboratory Medicine and Life Sciences, Wenzhou Medical University, Wenzhou, 325035, Zhejiang, China.
Purpose: Growing evidence suggests that the tyrosine phosphatase SHP2 is pivotal for tumor progression. Triple-negative breast cancer (TNBC) is the most lethal subtype of breast cancer, characterized by its high recurrence rate, aggressive metastasis, and resistance to chemotherapy. Understanding the mechanisms of tumorigenesis and the underlying molecular pathways in TNBC could aid in identifying new therapeutic targets.
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