Author
Listed:
- Thomas D. Pollard
(The Johns Hopkins University School of Medicine, Department of Cell Biology and Anatomy)
- Ueli Aebi
(The Johns Hopkins University School of Medicine, Department of Cell Biology and Anatomy)
- John A. Cooper
(The Johns Hopkins University School of Medicine, Department of Cell Biology and Anatomy)
- Marshall Elzinga
(Brookhaven National Laboratories, Biology Division)
- Walter E. Fowler
(The Johns Hopkins University School of Medicine, Department of Cell Biology and Anatomy)
- Linda M. Griffith
(The Johns Hopkins University School of Medicine, Department of Cell Biology and Anatomy)
- Ira M. Herman
(The Johns Hopkins University School of Medicine, Department of Cell Biology and Anatomy)
- John Heuser
(Washington University School of Medicine, Department of Physiology and Biophysics)
- Gerhard Isenberg
(The Johns Hopkins University School of Medicine, Department of Cell Biology and Anatomy)
- Daniel P. Kiehart
(The Johns Hopkins University School of Medicine, Department of Cell Biology and Anatomy)
- Janelle Levy
(The Johns Hopkins University School of Medicine, Department of Cell Biology and Anatomy)
- Susan MacLean-Fletcher
(The Johns Hopkins University School of Medicine, Department of Cell Biology and Anatomy)
- Pamela Maupin
(The Johns Hopkins University School of Medicine, Department of Cell Biology and Anatomy)
- Mark S. Mooseker
(Yale University, Department of Biology)
- Marschall Runge
(The Johns Hopkins University School of Medicine, Department of Cell Biology and Anatomy)
- P. Ross Smith
(New York University School of Medicine, Department of Cell Biology)
- Peter Tseng
(The Johns Hopkins University School of Medicine, Department of Cell Biology and Anatomy)
Abstract
Actin is one of the major proteins in eukaryotic cells, and actin filaments are the major structural element of both the contractile apparatus and the “cyto-skeleton” of most cells. In their role as a contractile protein, filaments of actin are thought to interact with myosin to generate the force for cellular motility, much like they do in muscle contraction. The role of actin as a structural protein is less well defined, but probably no less important. The general idea is that the cytoplasm contains a three-dimensional network of actin filaments that can be cross-linked to form a gel. This network forms an internal scaffolding that traps the organelles (see Mast, 1926), distributes local contractile forces throughout the cytoplasm to the cell surface, and may also provide a scaffolding for certain enzyme systems (Clark and Masters, 1975).
Suggested Citation
Thomas D. Pollard & Ueli Aebi & John A. Cooper & Marshall Elzinga & Walter E. Fowler & Linda M. Griffith & Ira M. Herman & John Heuser & Gerhard Isenberg & Daniel P. Kiehart & Janelle Levy & Susan Mac, 1982.
"The Mechanism of Actin-Filament Assembly and Cross-Linking,"
Springer Books, in: Robert M. Dowben & Jerry W. Shay (ed.), Cell and Muscle Motility, chapter 2, pages 15-44,
Springer.
Handle:
RePEc:spr:sprchp:978-1-4684-4037-9_2
DOI: 10.1007/978-1-4684-4037-9_2
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