Journal ArticleDOI
The GTPase dynamin binds to and is activated by a subset of SH3 domains.
Ivan Gout,Ritu Dhand,Ian Hiles,Michael J. Fry,George Panayotou,Pamela Das,Oanh Truong,Nicholas F. Totty,J. Justin Hsuan,Grant W. Booker,Iain D. Campbell,Michael D. Waterfield,Michael D. Waterfield +12 more
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TLDR
Dynamin GTPase activity is stimulated by several of the bound SH3 domains, suggesting that the function of the SH3 module is not restricted to protein-protein interactions but may also include the interactive regulation of GTP-binding proteins.About:Â
This article is published in Cell.The article was published on 1993-10-08. It has received 555 citations till now. The article focuses on the topics: Dynamin & Dynamin II.read more
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Dynasore, a Cell-Permeable Inhibitor of Dynamin
Eric Macia,Marcelo Ehrlich,Ramiro Massol,Emmanuel Boucrot,Christian Brunner,Tomas Kirchhausen +5 more
TL;DR: Dynamin acts at two steps during clathrin coat formation; GTP hydrolysis is probably needed at both steps; Dynasore acts as a potent inhibitor of endocytic pathways known to depend on dynamin by rapidly blocking coated vesicle formation within seconds of dynasore addition.
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Induction of mutant dynamin specifically blocks endocytic coated vesicle formation.
TL;DR: It is concluded that dynamin is specifically required for endocytic coated vesicle formation, and that its GTP binding and hydrolysis activities are required to form constricted coated pits and, subsequently, for coatedvesicle budding.
Journal ArticleDOI
Regulation, substrates and functions of src.
TL;DR: This review focuses on developments in the last 6-7 years, and cites data resulting from the isolation and characterization of SRC mutants, crystallographic studies of the structures of SH2, SH3 and tyrosine kinase domains, biochemical studies of Src kinase activity and binding properties, and the biology of transgenic and knockout mouse strains.
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Structural basis for the binding of proline-rich peptides to SH3 domains
TL;DR: It is concluded that SH3 domains recognize proline-rich motifs possessing the left-handed type II polyproline (PPII) helix conformation, and these motifs appear to function as a molecular scaffold, promoting the formation of the PPII helix.
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Modular binding domains in signal transduction proteins
TL;DR: The transduction of a signal is a change in form of the signal as it is passed from one carrier to another, and the signal transduction protein must be highly integrated, with all of the elements working together to send just the appropriate quanta of signal for the specific need.
References
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Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease.
TL;DR: In this article, the rat pancreas RNA was used as a source for the purification of alpha-amylase messenger ribonucleic acid (RBA) using 2-mercaptoethanol.
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A comprehensive set of sequence analysis programs for the VAX
TL;DR: A group of programs that will interact with each other has been developed for the Digital Equipment Corporation VAX computer using the VMS operating system.
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Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase.
D B Smith,Kevin S. Johnson +1 more
TL;DR: Plasmid expression vectors have been constructed that direct the synthesis of foreign polypeptides in Escherichia coli as fusions with the C terminus of Sj26, a 26-kDa glutathione S-transferase (GST; EC 2.5.1.18) encoded by the parasitic helminth Schistosoma japonicum.
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Signal transduction by receptors with tyrosine kinase activity
Axel Ullrich,Joseph Schlessinger +1 more
TL;DR: Cet article synthese montre comment des recepteurs membranaires a activite tyrosine kinase peuvent etre impliques dans la transduction and notamment jouent le role de signal de the transduction.
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The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors.
Anne J. Ridley,Alan Hall +1 more
TL;DR: Rho, a ras-related GTP-binding protein, rapidly stimulated stress fiber and focal adhesion formation when microinjected into serum-starved Swiss 3T3 cells, implying that rho is essential specifically for the coordinated assembly of focal adhesions and stress fibers induced by growth factors.