研究领域

Structural biology/structure and function of proteins and cellular organelles/X-ray crystallography. Affiliated with the Department of Molecular Biology/Princeton Institute for the Science and Technology of Materials (PRISM) and Program in Neuroscience.

The basis for movement and force generation in muscle and non-muscle cells is the actin-based microfilament system. Actin is a 43 kilo-dalton protein that has been highly conserved since the dawn of the eukaryotes over a billion years ago. Primordial precursor forms of actin and tubulin exist in bacteria, pointing to an even earlier origin for polymerizing proteins as generators of movement. Its emergence at the same time as the eukaryotic cell membrane, replacing the rigid cell walls of prokaryotes, enabled cells to exhibit a wide variety of dynamic shape variation at the cell edge. These movements are the structural basis for cell migration, tension generation, engulfment of other organisms, muscle contraction, and various modes of nutrient transport. Perhaps the most dynamic manifestation of the versatility of the actin microfilament system is the human nervous system, where cycles of polymerization and depolymerization of actin are an essential element of neural plastic ity. Schutt's laboratory has used x-ray crystallography, selected-site mutagenesis, and other biophysical techniques to reveal the structures and roles of actin-binding proteins. This large family of proteins, including profilin, gelsolin, actin depolymerization protein, tropomyosin, and myosin, controls the dynamic organization of the actin microfilament system. Recently, Schutt has become interested in the structural biology of human neuro-developmental disorders, such as autism, where genomic variation in genes for key actin-binding proteins are well-correlated with dysfunctional synaptic connections. The architectonic challenge of bridging human behavior to molecular changes in the human brain must involve a full realization of the potential of the actin microfilament system to continuously reorganize into functional structures at cell edge and inwards towards the cell nucleus.

近期论文

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Cytoskeleton 2010; 67(9): 599-607. Tropomyosin is a tetramer under physiological salt conditions. Lassing, I, Hillberg, L, Hoglund, A-S, Karlsson, R, Schutt, CE, Lindberg, U Seminars in Cancer Biology 2008; 18: 2-11. The Microfilament System and Malignancy. Lindberg, U, Karlsson, R, Lassing, I, Schutt, CE, Hoglund, A-S J. of Appl. Cryst. 2008; 41: 600-605. Protein Crystals can be Incommensurately Modulated. Lovelace, JJ, Murphy, CR, Daniels, L, Narayan, K, Schutt, CE, Lindberg, U, Svensson, C, Borgstahl, GEO J. of Mol. Bio . 2007; 370: 331-348. Molecular and Structural Basis for Redox Regulation of β-actin. Lassing, I, Schmitzberger, F, Bjornstedt, M, Holmgren, A, Nordlund, P, Schutt, C, Lindberg, U Eur. J. Cell Biol. 2006; 85: 399-409. Tropomyosins are present in lamellipodia of motile cells. Hillberg, L, Rathje, L-SZ Nyakern-Meazza, M, Helfand, B, Goldman, RD, Schutt, CE, Lindberg, U. Advances in Molecular and Cell Biology 2006; 37: 49-66. The Connection Between Actin ATPase and Polymerization. Schuler, H, Karlson, R, Schutt, CE, and Lindberg, U. J. of Appl. Cryst. 2004; 37: 327-330. Imaging Modulated Reflections From a Semi-Crystalline State of Profilin: Actin Crystals. Lovelace JJ, Narayan K, Chik JK, Bellamy HD, Snell EH, Lindberg U, Schutt CE, Borgstahl GEO FEBS Lett. 2003; 552 (2-3): 82-85. Activation in Isolation: Exposure of the Actin-Binding Site in the C-terminal Half of Gelsolin Does Not Require Actin. Narayan K, Chumnarnsilpa S, Choe H, Irobi E, Urosev D, Lindberg U, Schutt CE, Burtnick LD, Robinson RC J. Biol. Chem. 2002; 277 (32): 28774-28779. Tropomyosin and Gelsolin Cooperate in Controlling the Microfilament System. Nyakern-Meazza M, Narayan K, Schutt CE, Lindberg U J. Mol. Biol. 2002; 317 (4): 577-589. The Role of MeH73 in Actin Polymerization and ATP Hydrolysis. Nyman T, Schuler H, Korenbaum E, Schutt CE, Karlsson R, Lindberg U J. Biol. Chem. 2002; 277 (18): 15828-15833. A Cross-Linked Profilin-Actin Heterodimer Interferes With Elongation at the Fast-Growing End of F-Actin. Nyman T, Page R, Schutt CE, Karlsson R, Lindberg U Nucl. Acids Res. 2001; 29 (11): 2377-81. The Enhancement of PCR Amplification by Low Molecular Weight Amides. Chakrabarti R, Schutt CE J. Mol. Biol. 2000; 304 (5):861-871. Crystal Structure of the Oligomerization Domain of NSP4 from Rotavirus Reveals a Core Metal-Binding Site. Bowman GD, Nodelman IM, Levy O, Lin SL, Tian P, Zamb TJ, Udem SA, Venkataraghavan B, Schutt CE Anat. Rec. (New Anat.) 2000; 261:198-216. The New Architectonics: An Invitation To Structural Biology. Schutt CE and Lindberg U Proteins 2000; 41:374-384. A Comparative Structural Analysis of the ADF/Cofilin Family. Bowman GD, Nodelman IM, Chua NH, Lindberg U, Schutt CE FEBS Lett. 2000; 476 (3):155-159. Covalent Binding of ATPgS to the Nucleotide-Binding Site in S14C-actin. Schuler H, Schutt CE, Lindberg U, Karlsson R Eur. J. Biochem. 2000; 267 (13): 4054-4062. Mutational Analysis of Arginine 177 in the Nucleotide Binding Site of β-Actin. Schuler H, Nyakern M, Schutt CE, Lindberg U, Karlsson R Eur. J. Biochem. 2000; 267 (2): 476-486. Thermal Unfolding of G-actin Monitored with the DNase I-inhibition Assay; Stabilities of Actin Isoforms. Schuler H, Lindberg U, Schutt CE, Karlsson R J. Mol. Biol. 1999; 294 (5): 1271-1285. X-ray Structure Determination of Human Profilin II: A Comparative Structural Analysis of Human Profilins. Nodelman IM, Bowman GD, Lindberg U, Schutt CE Les Cahiers de Science & Vie 1999; 53: 78-87. Nouveau Regard Sur le Muscle. Kreatsoulas C, Lindberg U, Schutt CE