Publication Detail
The publication detail shows the title, authors (with indicators showing other profiled authors), information on the publishing organization, abstract and a link to the article in PubMed. This abstract is what is used to create the fingerprint of the publication. If any grants are referenced by the publication, they will be listed here as well.
Microfilaments and actin-associated proteins at sites of membrane-substrate attachment within acetylcholine receptor clusters.
R J Bloch; M Velez; J G Krikorian; D Axelrod (Profiled Author: Robert J Bloch)
Department of Physiology, University of Maryland School of Medicine, Baltimore 21201.
Experimental cell research 1989;182(2):583-96.
Rat myotubes in tissue culture form broad areas of close contact with the substrate. These areas often display two distinct, interdigitating sets of membrane domains. One, the "contact domain", is close to the substrate; the other, termed the "AChR domain", is further from the substrate and is rich in acetylcholine receptors (AChR). We have used fluorescence techniques to study the organization of the cytoskeleton in these areas. Substrate-apposed membrane of the myotubes was exposed either by shearing or by permeabilizing the cells with a neutral detergent. Phalloidin derivatives and affinity-purified polyclonal or monoclonal antibodies specific for cytoskeletal proteins were then applied to the samples. Sheared samples were observed by epifluorescence microscopy; detergent-permeabilized samples were observed by total internal reflection fluorescence microscopy. We found that, like antivinculin, fluorescent phalloidin derivatives and antibodies to alpha-actinin, filamin, and talin preferentially labeled the contact domains. This suggests that bundles of microfilaments associate with the membrane at sites of myotube-substrate attachment. In contrast, a 43K protein, closely associated with AChR, was present only at AChR domains. A monoclonal antibody to actin labeled both AChR and contact domains, suggesting that actin is enriched over both regions. Our results suggest that, like the plasma membrane of AChR clusters, the underlying membrane skeleton is organized into at least two distinct domains.
2 Originating Grant
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1.
BLOCH, ROBERT J
ADHESIVE MACROMOLECULES OF MUSCLE AND NERVE
1 July 1985 - 1 April 1989
NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE
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2.
Bloch, Robert J
Macromolecules Involved in Synapse Formation
1 April 1981 - 31 March 2007
NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE
Scientific Context
This section shows information related to the publication - computed using the fingerprint of the publication - including related publications, related experts and related grants with fingerprints representing significant amounts of overlap between their fingerprint and this publication. The red dots indicate whether those experts or terms appear within the publication, thereby showing potential and actual connections.
Related Publications
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1.
1990M P Daniels; J G Krikorian; A J Olek; R J Bloch
Experimental cell research 1990;186(1):99-108. -
2.
2007C Antolik; D H Catino; A M O'Neill; W G Resneck; J A Ursitti; R J Bloch
The actin binding domain of ACF7 binds directly to the tetratricopeptide repeat domains of rapsyn.
Neuroscience 2007;145(1):56-65. -
3.
1995A M Belkin; K Burridge
Experimental cell research 1995;221(1):132-40.
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