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Center for Basic Research in Digestive Diseases, Department of
Biochemistry and Molecular Biology, and Department of Molecular
Neuroscience, Mayo Clinic, Rochester, MN 55905
Communicated by Thomas S. Reese, National Institute of Neurological
Disorders and Stroke, Bethesda, MD, October 29, 1996
(received for review October 1995)
In the 7 years since dynamin was first isolated from bovine
brain in search of novel microtubule-based motors, our understanding of
this enzyme has expanded significantly. We now know that brain dynamin
belongs to a family of large GTPases, which mediate vesicle trafficking. Furthermore, this enzymatic activity is markedly increased
through association with microtubules, acidic phospholipids, and
certain regulatory proteins that contain Src homology 3 (SH3) domains.
From functional, genetic, and cellular manipulations, it is now
generally accepted that dynamin participates in the endocytic uptake of
receptors, associated ligands, and plasma membrane following an
exocytic event. These observations have confirmed at least one function
of dynamin that was predicted from seminal studies on a pleiotropic
mutant, shibirets
(shits) in Drosophila
melanogaster. Of equal interest is the finding that there are
multiple dynamin gene products, including two that are expressed in a
tissue-specific manner, and they share marked homology with a larger
family of distinct but related proteins. Therefore, it is attractive to
speculate that the different dynamins may participate in related
cellular functions, such as distinct endocytic processes and even
secretion. In turn, dynamin could play an important role in cell
growth, cell spreading, and neurite outgrowth. The purpose of this
review is to enumerate on the expansive dynamin literature and to
discuss the nomenclature, expression, and putative functions of this
growing and interesting family of proteins.
Proc. Natl. Acad. Sci. USA
Vol. 94,
pp. 377-384,
January 1997
Review
The dynamins: Redundant or distinct functions for an expanding family
of related GTPases?
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J. E. Pessin, D. C. Thurmond, J. S. Elmendorf, K. J. Coker, and S. Okada Molecular Basis of Insulin-stimulated GLUT4 Vesicle Trafficking. LOCATION! LOCATION! LOCATION! J. Biol. Chem., January 29, 1999; 274(5): 2593 - 2596. [Full Text] [PDF] |
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H.-W. Shin, H. Takatsu, H. Mukai, E. Munekata, K. Murakami, and K. Nakayama Intermolecular and Interdomain Interactions of a Dynamin-related GTP-binding Protein, Dnm1p/Vps1p-like Protein J. Biol. Chem., January 29, 1999; 274(5): 2780 - 2785. [Abstract] [Full Text] [PDF] |
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S. Ahn, S. Maudsley, L. M. Luttrell, R. J. Lefkowitz, and Y. Daaka Src-mediated Tyrosine Phosphorylation of Dynamin Is Required for beta 2-Adrenergic Receptor Internalization and Mitogen-activated Protein Kinase Signaling J. Biol. Chem., January 15, 1999; 274(3): 1185 - 1188. [Abstract] [Full Text] [PDF] |
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L Pelloquin, P Belenguer, Y Menon, N Gas, and B Ducommun Fission yeast Msp1 is a mitochondrial dynamin-related protein J. Cell Sci., January 11, 1999; 112(22): 4151 - 4161. [Abstract] [PDF] |
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D. C. Wienke, M. L.W. Knetsch, E. M. Neuhaus, M. C. Reedy, and D. J. Manstein Disruption of a Dynamin Homologue Affects Endocytosis, Organelle Morphology, and Cytokinesis in Dictyostelium discoideum Mol. Biol. Cell, January 1, 1999; 10(1): 225 - 243. [Abstract] [Full Text] |
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