James Spudich
Academic Appointments
Appointment
Organization
Professor
Professor
Member
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Curriculum Vitae Doc
Honors & Awards
Title
Organization
Date(s)
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
12 honors and awards: view full list
Administrative Appointments
Title
Organization
Start Year
End Year
Co-Founder and first Director, Interdisciplinary Program, Bio-X
Stanford University
1998
2002
Co-Founder
Cytokinetics, Inc
1998
-
Chairman, Department of Biochemistry
Stanford University School of Medicine
1994
1998
Professor, Department of Biochemistry
Stanford University School of Medicine
1992
-
Professor, Department of Developmental Biology
Stanford University School of Medicine
1989
-
10 appointments: view full list
Professional Education
Degree
Awarding Institution
Field of Study
Year of Graduation
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
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.
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
- Spudich JA, "Molecular Motors: A Surprising Twist in Myosin VI Translocation." Curr Biol 2008; 18: 2: R68-70 More »
- Dunn AR, Spudich JA "Dynamics of the unbound head during myosin V processive translocation." Nat Struct Mol Biol 2007; More »
- Liao JC, Spudich JA, Parker D, Delp SL "Extending the absorbing boundary method to fit dwell-time distributions of molecular motors with complex kinetic pathways." Proc Natl Acad Sci U S A 2007; 104: 9: 3171-6 More »
- Chen Q, Lakshmikanth GS, Spudich JA, De Lozanne A "The Localization of INCENP at the Cleavage Furrow Is Dependent on Kif12 and Involves Interactions of the N-Terminus of INCENP with the Actin Cytoskeleton." Mol Biol Cell 2007; More »
- Geething NC, Spudich JA "Identification of a minimal myosin Va binding site within an intrinsically unstructured domain of melanophilin." J Biol Chem 2007; More »
114 publications: view full list