Journal ArticleDOI
A vertebrate actin-related protein is a component of a multisubunit complex involved in microtubule-based vesicle motility
Reads0
Chats0
TLDR
Actin-RPV is a major component of the dynactin complex, an activator of dynein-driven vesicle movement, indicating that unlike conventional actins which work in conjunction with myosin motors, actin- RPV may be involved in cytoplasmic movements via a microtubule-based system.Citations
More filters
Journal ArticleDOI
A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
TL;DR: The results support a role for the striated muscle dystrophin-glycoprotein complex in linking the actin- based cytoskeleton with the extracellular matrix and suggest that dystophin and dystroglycan may play substantially different functional roles in nonmuscle tissues.
Journal ArticleDOI
Molecular characterization of the 50-kD subunit of dynactin reveals function for the complex in chromosome alignment and spindle organization during mitosis
TL;DR: Overexpression of p50 in COS-7 cells disrupted mitosis, causing cells to accumulate in a prometaphase-like state, and provide direct in vivo evidence for a role for vertebrate dynactin in modulating cytoplasmic dynein binding to an organelle.
Journal ArticleDOI
Purification of a Cortical Complex Containing Two Unconventional Actins from Acanthamoeba by Affinity Chromatography on Profilin-Agarose
TL;DR: Four polypeptides of 47, 44, 40, and 35 kD that bind to profilin-Sepharose and elute with high salt are identified and appear to be novel proteins.
Journal ArticleDOI
Cytoplasmic dynein binds dynactin through a direct interaction between the intermediate chains and p150Glued.
TL;DR: Findings identify a direct interaction between two specific component polypeptides and support a role for dynactin as a dynein "receptor" and suggest, however, that this interaction must be highly regulated.
Journal ArticleDOI
The structure of the dynactin complex and its interaction with dynein
Linas Urnavicius,Kai Zhang,Aristides G. Diamant,Carina Motz,Max A. Schlager,Minmin Yu,Nisha A. Patel,Carol V. Robinson,Andrew P. Carter +8 more
TL;DR: The reconstruction reveals how dynactin is built around a filament containing eight copies of the actin-related protein Arp1 and one of β-actin, which is capped at each end by distinct protein complexes, and its length is defined by elongated peptides that emerge from the α-helical shoulder domain.
References
More filters
Journal ArticleDOI
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
Journal Article
Cleavage of structural proteins during the assemble of the head of bacterio-phage T4
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products as mentioned in this paper.
Book
Antibodies: A Laboratory Manual
Ed Harlow,David P. Lane +1 more
TL;DR: A second edition of Antibodies: A Laboratory Manual is being published in September 2013, Revised, extended and updated by Edward Greenfield of the Dana-Farber Cancer Center, the material has been recast with extensive new information and new chapters have been added.
Journal ArticleDOI
High resolution two-dimensional electrophoresis of proteins.
TL;DR: This technique provides a method for estimation of the number of proteins made by any biological system and can resolve proteins differing in a single charge and consequently can be used in the analysis of in vivo modifications resulting in a change in charge.
Journal ArticleDOI
Primer-directed enzymatic amplification of DNA with a thermostable DNA polymerase
Randall Keichi Saiki,David H. Gelfand,Susanne Stoffel,Stephen J. Scharf,Russell Higuchi,Glenn Thomas Horn,Kary B. Mullis,Henry A. Erlich +7 more
TL;DR: A thermostable DNA polymerase was used in an in vitro DNA amplification procedure, the polymerase chain reaction, which significantly improves the specificity, yield, sensitivity, and length of products that can be amplified.