Chapter 31 Molecular modifications during nerve-muscle synapse formation

Rubin, Lee L.; Anthony, Donna T.; Englander, Libbe L.; Lappin, Richard I.; Lieberburg, Ivan

doi:10.1016/s0079-6123(08)61839-7

Neural Regeneration

1987

DOI: 10.1016/s0079-6123(08)61839-7

|View full text |Cite

Chapter 31 Molecular modifications during nerve-muscle synapse formation

Lee L. Rubin

Donna T. Anthony

Libbe L. Englander

et al.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...

Citation Types

Supporting

Mentioning

Contrasting

Year Published

1987

1992

Publication Types

Select...

Article5

Relationship

Self Cite0

Independent5

Authors

Journals

Cited by 7 publications

(1 citation statement)

References 24 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…These include alpha-actinin, filamin, vinculin, talin, an intermediate filament-like molecule, nonmuscle actin, a 300-kD protein, and a 58-kD protein (5-7, 19, 22, 23, 33, 47, 49, 56; reviewed in reference 20). In addition, a 43-kD AChR-associated protein, thought to be capable of binding to both the AChR (10) and actin (53), is concentrated near AChR clusters (8,21,42,46,50).…”

mentioning

confidence: 99%

A molecular defect in virally transformed muscle cells that cannot cluster acetylcholine receptors.

Anthony

Jacobs-Cohen

Marazzi

et al. 1988

The Journal of Cell Biology

View full text Add to dashboard Cite

Abstract. Muscle cells infected at the permissive temperature with temperature-sensitive mutants of Rous sarcoma virus and shifted to the non-permissive temperature form myotubes that are unable to cluster acetylcholine receptors (Anthony, D. T., S. M. Schuetze, and L. L. Rubin. 1984. Proc. Natl. Acad. Sci. USA. 81:2265-2269.). Work described in this paper demonstrates that the vitally-infected cells are missing a 37-kD peptide which reacts with an anti-tropomyosin antiserum. Using a monoclonal antibody specific for the missing peptide, we show that this tropomyosin is absent from fibroblasts and is distinct from smooth muscle tropomyosins. It is also different from the two previously identified striated muscle myofibrillar tropomyosins (alpha and beta). We suggest that, in normal muscle, this novel, non-myofibrillar, tropomyosin-like molecule is an important component of a cytoskeletal network necessary for cluster formation. characteristic feature of the vertebrate neuromuscular junction is its enormously high concentration of acetylcholine receptors (AChRs) I. AChRs are uniformly distributed along embryonic muscle fibers, but accumulate at high concentrations at junctional sites in response to innervation. This accumulation is probably initiated by a factor of neural origin (12,28,43). In mature muscle, clusters are maintained by a component of the muscle's basal lamina, which has been studied in some detail (11,39). How the muscle cell responds to molecules that induce clustering is not well understood, although it might be anticipated that cytoskeletal elements are involved. A variety of cytoskeletal molecules are present in either the postsynaptic region of adult muscle or beneath AChR clusters on cultured muscle cells. These include alpha-actinin, filamin, vinculin, talin, an intermediate filament-like molecule, nonmuscle actin, a 300-kD protein, and a 58-kD protein (5-7, 19, 22, 23, 33, 47, 49, 56; reviewed in reference 20). In addition, a 43-kD AChR-associated protein, thought to be capable of binding to both the AChR (10) and actin (53), is concentrated near AChR clusters (8,21,42,46,50).The mere presence of a cytoskeletal molecule, however, does not guarantee its participation in clustering. Other structural changes occur during muscle cell development that could also require cytoskeletal reorganization. For instance, the synaptic region of muscle is characterized by extensive membrane folds. In addition, we have shown that AChR clustering initiates the sub-membrane localization and immobilization of a set of myonuclei and Golgi apparatus. This process probably results from a cytoskeletal reorganiza- tion beneath the cluster (17). To establish that particular cytoskeletal molecules have a direct role in clustering, evidence of a more functional nature must be obtained.Previously, we reported that chick myotubes that are infected at the permissive temperature with a temperaturesensitive mutant (tsNY68) of Rous sarcoma virus (RSV) and allowed to fuse at the nonpermissive temperature do not cluster thei...

show abstract

mentioning

confidence: 99%

A molecular defect in virally transformed muscle cells that cannot cluster acetylcholine receptors.

Anthony

Jacobs-Cohen

Marazzi

et al. 1988

The Journal of Cell Biology

View full text Add to dashboard Cite

show abstract

Glucocorticoid increases acetylcholinesterase and organization of the postsynaptic membrane in innervated cultured human muscle

Askanas¹,

McFerrin²,

Park-Matsumoto³

et al. 1992

Experimental Neurology

View full text Add to dashboard Cite

Towards Understanding Skeletal Muscle Regeneration

Grounds

1991

Pathology - Research and Practice

331

205

View full text Add to dashboard Cite

scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.

Contact Info

hi@scite.ai

10624 S. Eastern Ave., Ste. A-614

Henderson, NV 89052, USA

Blog Terms and Conditions API Terms Privacy Policy Contact Cookie Preferences Do Not Sell or Share My Personal Information

Made with 💙 for researchers

Part of the Research Solutions Family.

Chapter 31 Molecular modifications during nerve-muscle synapse formation

Cited by 7 publications

References 24 publications

A molecular defect in virally transformed muscle cells that cannot cluster acetylcholine receptors.

A molecular defect in virally transformed muscle cells that cannot cluster acetylcholine receptors.

Glucocorticoid increases acetylcholinesterase and organization of the postsynaptic membrane in innervated cultured human muscle

Towards Understanding Skeletal Muscle Regeneration

Contact Info

Product

Resources

About