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		Search Text: Home/< Back ToThe Science/Cellular Physiology
  Cellular Physiology
    The primary research interest of the Laboratory of Cellular Physiology, led by Dr. Lois Greene, is in the formation and breakdown of normal and pathological protein complexes in the cell, with an emphasis on the role of molecular chaperones.
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          headshot of Dr. Lois Greene
  Lois Greene, Ph.D.
          Scientist Emeritus
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      Meet the Team
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  Senior Investigator Research Interests
            
  Research Interests
              Dr. Greene's primary research interest is in the formation and dissolution of normal and pathological protein complexes in the cell, with an emphasis on the role of molecular chaperones.The translation of mRNA into its corresponding amino acid chain is only the first step in a protein's life cycle. Although some proteins spontaneously fold into their correct three-dimensional structures to execute their functions, many more require the assistance of molecular chaperones to achieve their correct conformational states in complexes with other proteins and cellular membranes. Dr. Greene studies the role of molecular chaperones and their co-factors in the formation of vesicular compartments from clathrin-coated pits in the cellular membrane during endocytosis. She has applied her wealth of experience in the cell biology of protein folding and membrane trafficking toward deciphering the mechanisms of prion formation and propagation.Prions are a class of proteins that can adopt an altered conformational state that not only leads them to form aggregates known as amyloids, but also allows them to similarly corrupt their normally folded soluble counterparts in the cytoplasm. In yeast, there are approximately a dozen prions, and their propagation requires several molecular chaperones, including Hsp104. Dr. Greene's laboratory complements biochemical studies with fluorescence imaging to follow the process of prion propagation in real time. In tissue culture, she and her colleagues are studying the cellular prion protein PrPC and the propagation of its scrapie isoform PrPSc, the cause of bovine spongiform encephalopathy, also known as BSE or "mad cow" disease.True prions are defined by the fact that they are genetically identical to their non-prion protein counterparts, i.e. they are inherited and propagated entirely through protein-protein interactions and are interconvertible. However, it is becoming increasingly clear that many neurodegenerative diseases—such as Huntington's disease, amyotrophic lateral sclerosis (ALS), and others that are associated with abnormal protein aggregation initiated through genetic mutations—have a prion-like component to their transmission. Once such proteins are misfolded, they may provide a template for other proteins to misfold. Moreover, these misfolded templates could be transmitted between cells. If correct, such a cumulative model of neurodegenerative transmission could partially account for the relatively late onset of these diseases.Dr. Greene and her colleagues are delving into this new paradigm to question how cells transmit misfolded proteins. Why, for example, is such an abnormal and potentially harmful protein aggregate not simply shunted off to the lysosome for degradation? How in turn does this abnormal protein move between cells? These are cellular trafficking questions that Dr. Greene's laboratory is well poised to address. Aggregates are carried as cargo by membrane vesicles and can be microscopically visualized in different cellular compartments by association with known molecular markers. Their passage can also be studied by genetic and RNAi methods that disrupt different steps in vesicular trafficking. Dr. Greene will complement this research with genetic studies of both the normal and mutant forms of the huntingtin gene in yeast and mammalian cells. Answering these questions will shed insight into the cellular pathophysiology of Huntington's disease and other protein aggregation disorders, which could lead to better understanding of these disorders on a broader scale.
  Featured Publications
                Mechanisms for Curing Yeast Prions.
            Authors:Greene LE, Saba F, Silberman RE, Zhao X.
                                                                                                                        
            Int J Mol Sci.
      
                2020 Sep 07;21(18):6536
        Read Publication
                      Mutations Outside the Ure2 Amyloid-Forming Region Disrupt [URE3] Prion Propagation and Alter Interactions with Protein Quality Control Factors.
            Authors:Kumar S, Dine EA, Paddock E, Steinberg DN, Greene LE, Masison DC.
                                                                                                                        
            Mol Cell Biol.
      
                2020 Oct 13;40(21):e00294-20
        Read Publication
                      Real-time imaging of yeast cells reveals several distinct mechanisms of curing of the [URE3] prion.
            Authors:Zhao X, Lanz J, Steinberg D, Pease T, Ahearn JM, Bezsonov EE, Staguhn ED, Eisenberg E, Masison DC, Greene LE.
                                                                                                                        
            J Biol Chem.
      
                2018 Mar 02;293(9):3104-3117
        Read Publication
                      Curing of [PSI+] by Hsp104 Overexpression: Clues to solving the puzzle.
            Authors:Greene LE, Zhao X, Eisenberg E.
                                                                                                                        
            Prion.
      
                2018 Jan 02;12(1):9-15
        Read Publication
                      Heat shock protein 104 (Hsp104)-mediated curing of [PSI(+)] yeast prions depends on both [PSI(+)] conformation and the properties of the Hsp104 homologs.
            Authors:Zhao X, Rodriguez R, Silberman RE, Ahearn JM, Saidha S, Cummins KC, Eisenberg E, Greene LE.
                                                                                                                        
            J Biol Chem.
      
                2017 May 26;292(21):8630-8641
        Read Publication
                                View More Publications
  Meet the Team

    headshot of Dr. Lois Greene

            Lois Greene, Ph.D.
                Scientist Emeritus
                Lois Greene earned a M.S. in environmental science from Washington State University in 1972, followed by a Ph.D. in biochemistry in 1975. She completed her postdoctoral fellowship at Washington State University before joining the NHLBI as a staff fellow in 1976. She became a Senior Investigator in the Laboratory of Cell Biology in 1982 and has been Chief of the Section of Cellular Physiology since 2002. Dr. Greene has authored or coauthored more than 100 papers. She holds memberships in the Biophysical Society and American Society for Biochemistry and Molecular Biology.
    
          Contact the lab
    50 South DrBethesda, MD 20814United States
        Phone:
                    301-496-1228
                Fax:
            301-402-1519
  Xiaohong Zhao
    
            Xiaohong Zhao, Ph.D.
        

    Biologist

        zhaox2@mail.nih.gov
            Yang-In Yim
    
            Yang-In Yim, Ph.D.
        

    Staff Scientist

        yimy@mail.nih.gov
            Olszewski
    
            Maciej Olszewski, Ph.D.
        

    Postdoctoral Fellow

        olszewskimb@mail.nih.gov
            Saidha
    
            Sheela Saidha, B.Sc.
        

    Postbaccalaureate

        saidhas@nhlbi.nih.gov Back To Top Link
  

        

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