Induction of mutant dynamin specifically blocks endocytic coated vesicle formation. (1994)

by H Damke, T Baba, D E Warnock, S L Schmid
Venue:J. Cell Biol.
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Dynamin at the neck of caveolae mediates their budding to form transport vesicles by GTP-driven fission from the plasma membrane of endothelium

by Phil Oh, Deirdre P. Mcintosh, Jan E. Schnitzer - J Cell Biol , 1998
"... The molecular mechanisms mediating cell surface trafficking of caveolae are unknown. Caveolae bud from plasma membranes to form free carrier vesi-cles through a “pinching off ” or fission process requiring cytosol and driven by GTP hydrolysis (Schnitzer, J.E., ..."
Abstract - Cited by 126 (1 self) - Add to MetaCart
The molecular mechanisms mediating cell surface trafficking of caveolae are unknown. Caveolae bud from plasma membranes to form free carrier vesi-cles through a “pinching off ” or fission process requiring cytosol and driven by GTP hydrolysis (Schnitzer, J.E.,
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Dynamin-mediated internalization of caveolae

by John R. Henley, Eugene W. A. Krueger, Barbara J. Oswald, Mark A. Mcniven - J. Cell Biol , 1998
"... Abstract. The dynamins comprise an expanding family of ubiquitously expressed 100-kD GTPases that have been implicated in severing clathrin-coated pits during receptor-mediated endocytosis. Currently, it is unclear whether the different dynamin isoforms perform redundant functions or participate in ..."
Abstract - Cited by 98 (11 self) - Add to MetaCart
Abstract. The dynamins comprise an expanding family of ubiquitously expressed 100-kD GTPases that have been implicated in severing clathrin-coated pits during receptor-mediated endocytosis. Currently, it is unclear whether the different dynamin isoforms perform redundant functions or participate in distinct endocytic processes. To define the function of dynamin II in mammalian epithelial cells, we have generated and characterized peptide-specific antibodies to domains that either are unique to this isoform or conserved within the dynamin family. When microinjected into cultured hepatocytes these affinity-purified antibodies inhibited clathrin-mediated endocytosis and induced the formation of long plasmalemmal invaginations with attached clathrin-coated pits. In addition, clusters of Eukaryotic cells internalize plasma membrane, surface receptors, and small molecules via several distinct endocytic processes (reviewed in Anderson
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Dynasore, a cell-permeable inhibitor of dynamin

by Eric Macia, Marcelo Ehrlich, Ramiro Massol, Emmanuel Boucrot, Christian Brunner, Tomas Kirchhausen - Dev. Cell , 2006
"... 0change that accompanies GAP-stimulated GTP hydroly-sis leads to neck constriction and scission ([Danino et al., 2004]; reviewed by Danino and Hinshaw [2001]). In the regulatory models, dynamin works like other GTPases as a time-limited recruiting agent. The regula-tory models come principally from ..."
Abstract - Cited by 94 (3 self) - Add to MetaCart
0change that accompanies GAP-stimulated GTP hydroly-sis leads to neck constriction and scission ([Danino et al., 2004]; reviewed by Danino and Hinshaw [2001]). In the regulatory models, dynamin works like other GTPases as a time-limited recruiting agent. The regula-tory models come principally from studies on overex-pression of dynamin mutants defective in self-assembly
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Differential distribution of dynamin isoforms in mammalian cells. Mol Biol Cell 9:2595–2609

by Hong Cao, Fabiana Garcia, Mark A. Mcniven, Juan S. Bonifacino , 1998
"... Dynamins are 100-kDa GTPases that are essential for clathrin-coated vesicle formation during receptor-mediated endocytosis. To date, three different dynamin genes have been identified, with each gene expressing at least four different alternatively spliced forms. Currently, it is unclear whether the ..."
Abstract - Cited by 86 (11 self) - Add to MetaCart
Dynamins are 100-kDa GTPases that are essential for clathrin-coated vesicle formation during receptor-mediated endocytosis. To date, three different dynamin genes have been identified, with each gene expressing at least four different alternatively spliced forms. Currently, it is unclear whether these different dynamin gene products perform distinct or redundant cellular functions. Therefore, the focus of this study was to identify additional spliced variants of dynamin from rat tissues and to define the distribution of the dynamin family members in a cultured rat epithelial cell model (Clone 9 cells). After long-distance reverse transcription (RT)-PCR of mRNA from different rat tissues, the full-length cDNAs encoding the different dynamin isoforms were sequenced and revealed four additional spliced variants for dynamin I and nine for dynamin III. Thus, in rat tissues there are a total of at least 25 different mRNAs produced from the three dynamin genes. Subsequently, we generated stably transfected Clone 9 cells expressing full-length cDNAs of six different spliced forms tagged with green fluorescent protein. Confocal or fluorescence microscopy of these transfected cells revealed that many of the dynamin proteins associate with distinct membrane compartments, which include clathrin-coated pits at the plasma membrane and the Golgi apparatus, and several undefined vesicle populations. These results indicate that the dynamin family is more extensive than was originally predicted and suggest that the different dynamin proteins are localized to distinct cytoplasmic or membrane compartments.
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The dynamin-related GTPase, Dnm1p, controls mitochondrial morphology in yeast

by Denichiro Otsuga, Brian R. Keegan, Ellen Brisch, John W. Thatcher, Greg J. Hermann, William Bleazard, Janet M. Shaw - J. Cell , 1998
"... Abstract. The Saccharomyces cerevisiae Dnm1 protein is structurally related to dynamin, a GTPase required for membrane scission during endocytosis. Here we show that Dnm1p is essential for the maintenance of mitochondrial morphology. Disruption of the DNM1 gene causes the wild-type network of tubula ..."
Abstract - Cited by 78 (9 self) - Add to MetaCart
Abstract. The Saccharomyces cerevisiae Dnm1 protein is structurally related to dynamin, a GTPase required for membrane scission during endocytosis. Here we show that Dnm1p is essential for the maintenance of mitochondrial morphology. Disruption of the DNM1 gene causes the wild-type network of tubular mitochondrial membranes to collapse to one side of the cell but does not affect the morphology or distribution of other cytoplasmic organelles. Dnm1 proteins containing point mutations in the predicted GTP-binding domain or completely lacking the GTP-binding domain fail to rescue mitochondrial morphology defects in a dnm1 mutant and induce dominant mitochondrial morphology defects in wild-type cells. Indirect immunofluorescence reveals that Dnm1p is distributed in punctate
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The clathrin endocytic pathway in viral infection

by Louis Detulleo, Tomas Kirchhausen - EMBO J , 1998
"... How important is the clathrin-dependent endocytic pathway for entry of viruses into host cells? While it is widely accepted that Semliki Forest virus (SFV), an enveloped virus, requires this pathway there are conflicting data concerning the closely related Sindbis virus, as well as varying results w ..."
Abstract - Cited by 77 (1 self) - Add to MetaCart
How important is the clathrin-dependent endocytic pathway for entry of viruses into host cells? While it is widely accepted that Semliki Forest virus (SFV), an enveloped virus, requires this pathway there are conflicting data concerning the closely related Sindbis virus, as well as varying results with picornaviruses such as human rhinovirus 14 (HRV 14) and poliovirus. We have examined the entry mode of SFV, Sindbis virus, HRV 14 and poliovirus using a method that identifies single infected cells. This assay takes advantage of the observation that the clathrindependent endocytic pathway is specifically and potently arrested by overexpression of dynamin mutants that prevent clathrin-coated pit budding. Using HeLa cells and conditions of low multiplicity of infection to favor use of the most avid pathway of cell entry, it was found that SFV, Sindbis virus and HRV 14 require an active clathrin-dependent endocytic pathway for successful infection. In marked contrast, infection of HeLa cells by poliovirus did not appear to require the clathrin pathway.
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Infectious entry pathway of adeno-associated virus and adeno-associated virus vectors

by Jeffrey S. Bartlett, Rose Wilcher, R. Jude Samulski, Jeffrey S. Bartlett, Rose Wilcher, R. Jude Samulski , 2000
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Abstract - Cited by 76 (5 self) - Add to MetaCart
Updated information and services can be found at:
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Clathrin-independent pinocytosis is induced in cells overexpressing a temperaturesensitive mutant of dynamin

by Hanna Damke, Takeshi Baba, Ra L. Schmid - J. Cell , 1995
"... Abstract. A stable HeLa cell line expressing a dynamin mutant, dyn ts, exhibits a temperature-sensitive defect in endocytic clathrin-coated vesicle formation. Dyn ts carries a point mutation, G273D, corresponding to the Drosophila shibire tsl allele. The ts-defect in receptormediated endocytosis sho ..."
Abstract - Cited by 74 (1 self) - Add to MetaCart
Abstract. A stable HeLa cell line expressing a dynamin mutant, dyn ts, exhibits a temperature-sensitive defect in endocytic clathrin-coated vesicle formation. Dyn ts carries a point mutation, G273D, corresponding to the Drosophila shibire tsl allele. The ts-defect in receptormediated endocytosis shows a rapid onset (<5 min) and is readily reversible. At the nonpermissive temperature (38°C) HRP uptake is only partially inhibited. Moreover, when cells are held at the nonpermissive temperature, fluid phase uptake fully recovers to wildtype levels within 30 min, while receptor-mediated en-docytosis remains inhibited. The residual HRP uptake early after shift to the nonpermissive temperature and the induced HRP uptake that occurs after recovery are insensitive to cytosol acidification under conditions that
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Limited entry of adenovirus vectors into well-differentiated airway epithelium is responsible for inefficient gene transfer

by Raymond J. Pickles, Douglas Mccarty, Hirotoshi Matsui, J. Hart, Scott H. R, Richard C. Boucher, Updated Information, Raymond J. Pickles, Douglas Mccarty, Hirotoshi Matsui, Pádraig J. Hart, Scott H. Randell, Richard C. Boucher - J. Virol , 1998
"... These include: This article cites 32 articles, 13 of which can be accessed free at: ..."
Abstract - Cited by 54 (6 self) - Add to MetaCart
These include: This article cites 32 articles, 13 of which can be accessed free at:
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Redundant and distinct functions for dynamin-1 and dynamin-2 isoforms

by Yoram Altschuler, Shana M. Barbas, Laura J. Terlecky, Kitty Tang, Stephen Hardy, Keith E. Mostov, Ra L. Schmid - J. Cell Biol , 1998
"... Abstract. A role for dynamin in clathrin-mediated endocytosis is now well established. However, mammals express three closely related, tissue-specific dynamin isoforms, each with multiple splice variants. Thus, an important question is whether these isoforms and splice variants function in vesicle f ..."
Abstract - Cited by 53 (2 self) - Add to MetaCart
Abstract. A role for dynamin in clathrin-mediated endocytosis is now well established. However, mammals express three closely related, tissue-specific dynamin isoforms, each with multiple splice variants. Thus, an important question is whether these isoforms and splice variants function in vesicle formation from distinct intracellular organelles. There are conflicting data as to a role for dynamin-2 in vesicle budding from the TGN. To resolve this issue, we compared the effects of overexpression of dominant-negative mutants of dynamin-1 (the neuronal isoform) and dynamin-2 (the ubiquitously expressed isoform) on endocytic and biosynthetic membrane trafficking in HeLa cells and polarized MDCK cells. Both dyn1(K44A) and dyn2(K44A) were potent inhibitors of receptor-mediated endocytosis;
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