Key Documents
James Spudich
- Professor, Biochemistry
- Professor, Developmental Biology
- Member, Bio-X
- Member, Cancer Center
Contact Information
- Academic Offices
Personal Information Email jspudich@stanford.edu Tel (650) 723-7634
Administrative Appointments
- Co-Founder and first Director, Interdisciplinary Program, Bio-X, Stanford University , (1998– 2002 )
- Co-Founder, Cytokinetics, Inc , (1998– present )
- Chairman, Department of Biochemistry, Stanford University School of Medicine , (1994– 1998 )
- Professor, Department of Biochemistry, Stanford University School of Medicine , (1992– present )
- Professor, Department of Developmental Biology, Stanford University School of Medicine , (1989– present )
- Chairman, Department of Structural Biology, Stanford University School of Medicine , (1979– 1984 )
- Professor, Department of Structural Biology, Stanford University School of Medicine , (1977– 1992 )
- Professor, Department of Biochemistry and Biophysics, University of California, San Francisco , (1976– 1977 )
- Associate Professor, Department of Biochemistry & Biophysics, University of California, San Francisco , (1974– 1976 )
- Assistant Professor, Department of Biochemistry & Biophysics, University of California, San Francisco , (1971– 1974 )
Honors and Awards
- U.S. Genomics Award for Outstanding Investigator in the field of Single Molecule Biology, Biophysical Society (2006)
- Named the "Douglass M. and Nola Leishman Professor of Cardiovascular Disease", Stanford University (1987 - present)
- Elected Member of the National Academy of Sciences, the National Academy of Sciences (1991)
- American Heart Association Research Prize, National American Heart Association (1991)
- Alexander von Humboldt Research Award, Alexander von Humboldt Research Foundation (1991)
- NIH Merit Award, National Institutes of Health (1991)
- External Scientific Member of the Max-Planck-Institute für Biochemie in Martinsried bei München, Max-Planck Society (1994)
- Biophysical Society Lifetime Research Career Award, Biophysical Society (1995)
- Lewis S. Rosenstiel Award, Brandeis University (1996)
- 1997 Repligen Award in Chemistry of Biological Processes, Division of Biological Chemistry of the American Chemical Society (1996)
- Elected Fellow of the American Academy of Arts and Sciences, the American Academy of Arts and Sciences (1997)
- Elected Fellow of the American Association for the Advancement of Science, the American Association for the Advancement of Science (2001)
Professional Education
- B.S., University of Illinois Chemistry (1963)
- Ph.D., Stanford University Biochemistry (1968)
- Postdoctoral, Stanford University Genetics (1969)
- Postdoctoral, Cambridge University, MRC LMB Structural Biology (1971)
Postdoctoral Advisees
Industry Relationships
Stanford is committed to ethical and transparent interactions with our industry partners. It is our policy to disclose payments of $5,000 or more, equity valued at $5,000 or more in a publicly traded company, or any equity in a privately held company, to physicians and scientists employed by Stanford University from companies or other commercial entities with which they interact as part of their professional activities.
- Consulting: Cytokinetics, Inc.
- Equity: Cytokinetics, Inc.
- Service on Board of Directors: Cytokinetics, Inc.
Research Interests
The general research interest of this laboratory is the molecular basis of cell motility. We have three specific research interests, the molecular basis of energy transduction that leads to ATP-driven myosin movement on actin, the biochemical basis of the regulation of actin and myosin interaction and their assembly states, and the roles these proteins play in vivo, in cell movement and changes in cell shape.
We work on two experimental systems: contraction of mammalian muscle and chemotaxis of Dictyostelium discoideum cells. Each of these systems has its special advantages. Skeletal muscle has the most highly organized contractile apparatus of any cell type, and the chemistry and biochemistry of muscle actin and myosin are most advanced.
Dictyostelium discoideum, the cell that commands most of our attention, exhibits all of the behavior of nonmuscle mammalian cells and, unlike other eukaryotic cells, can be grown in large amounts for biochemical work. Furthermore, DNA-mediated transformation is being applied to this organism, and we have demonstrated efficient gene targeting by homologous recombination in the myosin gene, which we have cloned and sequenced.
Our approaches include biochemical and structural studies of actin, myosin, and associated regulatory proteins. In addition, we have designed and developed in vitro assays for ATP-dependent movement of purified myosin on filaments reconstituted from purified actin. These assays allow us to analyze mutant myosin molecules for altered function. The site-directed mutagenized forms of myosin are obtained by gene cloning and expression in an appropriate host. Our demonstration that the Dictyostelium discoideum myosin gene can undergo homologous recombination allows us to also probe the effects of the altered myosin forms on the phenotype of the cell.
Publications
- J Mol Biol. 2009; (4): 862-7
- Biophys J. 2008; (11): 5003-4
- Nat Struct Mol Biol. 2008; (6): 591-7
- Curr Biol. 2008; (2): R68-70
- Nat Struct Mol Biol. 2007; (3): 246-8
- PLoS Biol. 2007; (8): e210
- J Mol Biol. 2007; (5): 1361-73
- Mol Biol Cell. 2007; (9): 3366-74
- J Biol Chem. 2007; (29): 21518-28
- Proc Natl Acad Sci U S A. 2007; (9): 3171-6
- Proc Natl Acad Sci U S A. 2007; (3): 772-7
- PLoS One. 2006; e131
- Cell. 2006; (2): 242-4
- Biophys J. 2006; (2): 668-71
- Proc Natl Acad Sci U S A. 2005; (39): 13873-8
- Mol Cell. 2005; (4): 603-9
- Proc Natl Acad Sci U S A. 2005; (38): 13473-8
- Proc Natl Acad Sci U S A. 2005; (5): 1419-23
- Nat Struct Mol Biol. 2004; (9): 884-7
- Cell. 2004; (5): 737-49
- Proc Natl Acad Sci U S A. 2004; (47): 16519-24
- Proc Natl Acad Sci U S A. 2004; (45): 15825-6
- PLoS Biol. 2004; (11): e356
- Methods Enzymol. 2003; 112-33
- J Biol Chem. 2003; (2): 1229-38
- Proc Natl Acad Sci U S A. 2002; (22): 14159-64
- BMC Cell Biol. 2002; 19
- BMC Cell Biol. 2002; 4
- J Biol Chem. 2002; (11): 9088-95
- Nat Rev Mol Cell Biol. 2001; (5): 387-92
- Proc Natl Acad Sci U S A. 2001; (24): 13655-9
- J Biol Chem. 2001; (22): 19491-4
- Nat Cell Biol. 2001; (3): 311-5
- Methods. 2000; (4): 373-81
- Cell. 2000; (5): 683-94
- J Muscle Res Cell Motil. 2000; (2): 139-51
- J Cell Biol. 2000; (4): 823-38
- Proc Natl Acad Sci U S A. 2000; (17): 9482-6
- Trends Cell Biol. 2000; (6): 228-37
- FEBS Lett. 2000; (2-3): 267-72
- J Biol Chem. 1999; (21): 14517-20
- Biochemistry. 1999; (12): 3785-92
- J Mol Biol. 1999; (1): 173-85
- Science. 1999; (5408): 1689-95
- Nature. 1999; (6744): 590-3
- J Cell Biol. 1999; (5): 1039-48
- Methods Enzymol. 1998; 436-59
- Proc Natl Acad Sci U S A. 1998; (22): 12844-7
- Proc Natl Acad Sci U S A. 1998; (22): 13000-5
- Proc Natl Acad Sci U S A. 1998; (23): 13652-7
- FEBS Lett. 1998; (1-2): 23-7
- Methods Cell Biol. 1998; 47-69
- Biochemistry. 1998; (19): 6738-44
- Mol Cell. 1998; (7): 1043-50
- Biochemistry. 1998; (27): 9679-87
- Mol Biol Cell. 1997; (12): 2605-15
- Mol Biol Cell. 1997; (12): 2617-29
- Proc Natl Acad Sci U S A. 1997; (15): 7927-31
- FEBS Lett. 1997; (2): 233-8
- Biochemistry. 1997; (28): 8465-73
- J Struct Biol. 1997; (2): 189-201
- J Cell Biol. 1996; (6): 1277-91
- Genetics. 1996; (2): 801-10
- Mol Biol Cell. 1996; (7): 1123-36
- Development. 1996; (10): 3295-305
- Proc Natl Acad Sci U S A. 1996; (22): 12321-6
- EMBO J. 1996; (22): 6075-83
- Proc Natl Acad Sci U S A. 1996; (1): 443-6
- Annu Rev Cell Dev Biol. 1996; 543-73
- Genetics. 1995; (2): 505-15
- Biophys J. 1995; (4 Suppl): 291S-296S; discussion 296S-297S
- Curr Opin Struct Biol. 1995; (2): 181-6
- Curr Opin Cell Biol. 1995; (1): 89-93
- Cold Spring Harb Symp Quant Biol. 1995; 783-91
- Cell Motil Cytoskeleton. 1995; (1): 73-84
- Nature. 1994; (6506): 515-8
- J Cell Sci. 1994; 2875-86
- Development. 1994; (9): 2651-60
- J Biol Chem. 1994; (29): 18773-80
- Nature. 1994; (6471): 567-9
- Nature. 1994; (6467): 113-9
- Science. 1993; (5141): 1867-70
- Cell. 1993; (2): 363-71
- Methods Cell Biol. 1993; 1-21
- Proc Natl Acad Sci U S A. 1993; (2): 659-63
- Mol Biol Cell. 1993; (2): 233-46
- Mol Biol Cell. 1992; (12): 1455-62
- Annu Rev Biochem. 1992; 721-59
- Proc Natl Acad Sci U S A. 1992; (10): 4466-70
- Proc Natl Acad Sci U S A. 1992; (13): 5877-81
- Nature. 1991; (6333): 307-11
- Trends Genet. 1991; (5): 161-6
- J Cell Biol. 1991; (4): 677-88
- J Biol Chem. 1991; (24): 16044-9
- J Cell Sci Suppl. 1991; 129-33
- Curr Opin Genet Dev. 1991; (3): 378-82
- Ann N Y Acad Sci. 1990; 147-55
- Proc Natl Acad Sci U S A. 1990; (20): 8110-4
- Proc Natl Acad Sci U S A. 1990; (18): 7130-4
- J Biol Chem. 1990; (23): 13818-24
- J Mol Biol. 1990; (3): 699-710
- Mol Cell Biol. 1990; (7): 3578-83
- Dev Biol. 1990; (2): 359-67
- Curr Opin Cell Biol. 1990; (1): 116-20
- J Cell Biol. 1990; (1): 63-70
- Science. 1989; (4930): 656-8
- Cell Regul. 1989; (1): 55-63
- Cell Regul. 1989; (1): 1-11
- Nature. 1989; (6242): 549-51
- Nature. 1989; (6238): 154-6
- J Biol Chem. 1989; (25): 15144-50
- EMBO J. 1989; (3): 923-32
- Mol Cell Biol. 1989; (5): 1965-8
- J Cell Biol. 1989; (1): 203-10
- Nucleic Acids Res. 1988; (14A): 6617-35
- J Cell Biol. 1987; (6 Pt 2): 2999-3005
- Annu Rev Cell Biol. 1987; 379-421