MSGID: 1:317/3 64ae2c71   
   PID: hpt/lnx 1.9.0-cur 2019-01-08   
   TID: hpt/lnx 1.9.0-cur 2019-01-08   
    Newly identified protein regulates the creation of cellulose in plant   
   cells    
      
     Date:   
         July 11, 2023   
     Source:   
         Penn State   
     Summary:   
         A team has identified a protein that modifies the cellular machinery   
         responsible for producing cellulose, which could inform the design   
         of more stable, cellulose-enriched materials for biofuels and   
         other functions.   
      
      
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   Cellulose -- an integral component of plant cell walls -- is an important   
   source of food, paper, textiles and biofuels, but how its creation is   
   regulated within plant cells has remained unclear. Now, a team led by   
   researchers at Penn State has identified a protein that modifies the   
   cellular machinery responsible for producing cellulose, which ultimately   
   lends stability to that machinery.   
      
   This new understanding could inform the design of more stable, cellulose-   
   enriched materials for biofuels and other functions.   
      
   Within a plant cell, a complex of proteins called the cellulose synthase   
   complex builds a chain of cellulose. Regulation of this process determines   
   a variety of properties like when and how quickly it occurs as well as   
   the length of the cellulose chain.   
      
   "Cellulose is the most abundant biopolymer on Earth, yet despite   
   its importance, relatively little is known about how its synthesis is   
   regulated," said Ying Gu, professor of biochemistry and molecular biology   
   in the Penn State Eberly College of Science and leader of the research   
   team. "In this study, we identified a protein called calcium-dependent   
   protein kinase 32 (CPK32) and confirmed that it chemically modifies one   
   of the proteins in the cellulose synthase complex, ultimately helping   
   to regulate the cellulose biosynthesis process."  The researchers   
   published their findings in a paper appearing July 11 in the journal   
   New Phytologist.   
      
   The chemical modification carried out by the CPK32 protein is called   
   phosphorylation; it adds a chemical compound known as a phosphor group   
   to the cellulose synthase protein CESA3. These types of modifications   
   are reversible and support a variety of important biological functions   
   in the cell. In humans, more than 200,000 locations on proteins can be   
   phosphorylated by more than 500 proteins, which are called kinases. In   
   the plant Arabidopsis, also known as thale cress and commonly used in   
   plant science, more than 43,000 locations can be phosphorylated by more   
   than 1,000 kinases.   
      
   "Identifying which of the many kinases could phosphorylate cellulose   
   synthase was very daunting," said Gu. "We used a screening approach to   
   look for proteins that directly associate with CESA3. This revealed   
   the kinase CPK32, and we followed up with a series of experiments   
   to confirm that CPK32 actually phosphorylates CESA3, to identify the   
   specific location on CESA3 where this occurs, and to determine how this   
   phosphorylation impacts the plant."  The researchers then created a   
   version of the CESA3 protein with a mutation that altered the site where   
   the phosphor group is added, preventing phosphorylation. Cells of the   
   mutated plants -- where phosphorylation of CESA3 was not possible --   
   had reduced cellulose content and reduced stability of the cellulose   
   synthase complex, and adult plants of mutated plants had stunted growth.   
      
   "Previous studies have shown CPK32 plays a role in several biological   
   processes, including pollen tube growth as well as shoot and root   
   development," said Gu. "Here, we demonstrate a new function of CPK32   
   and a novel mechanism of phosphorylation in stabilizing the cellulose   
   synthase complex."  Next, the researchers plan to investigate whether   
   the phosphorylation of CESA3 is unique to CPK32 or if any other kinases   
   within the same family can similarly regulate cellulose biosynthesis.   
      
   "By regulating the stability of the cellulose synthase complex, we may be   
   able to encourage cells to produce longer cellulose chains and ultimately   
   engineer cellulose-rich materials," said Gu.   
      
   In addition to Gu, the research team at Penn State includes Xiaoran Xin,   
   graduate student in the Biochemistry, Microbiology and Molecular Biology   
   program at the time of the research; Donghui Wei, graduate student in   
   plant biology; Lei Lei, graduate student in plant biology at the time   
   of the research; and Shundai Li, assistant professor of biochemistry   
   and molecular biology. The research team also includes Haiyan Zheng at   
   Rutgers University and Ian Wallace at the University of Nevada, Reno.   
      
   This research was supported by the Center for Lignocellulose Structure   
   and Formation, an Energy Frontier Research Center funded by the   
   U.S. Department of Energy; the Penn State Department of Biochemistry   
   and Molecular Biology; and the National Science Foundation.   
      
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   Source: Materials provided by Penn_State. Original written by Gail   
   McCormick. Note: Content may be edited for style and length.   
      
      
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   Journal Reference:   
      1. Xiaoran Xin, Donghui Wei, Lei Lei, Haiyan Zheng, Ian S. Wallace,   
      Shundai   
         Li, Ying Gu. CALCIUM‐DEPENDENT PROTEIN KINASE32 regulates   
         cellulose biosynthesis through post‐translational modification   
         of cellulose synthase. New Phytologist, 2023; DOI: 10.1111/nph.19106   
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   Link to news story:   
   https://www.sciencedaily.com/releases/2023/07/230711130631.htm   
      
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