Developmental regulation of membrane traffic organization during synaptogenesis in mouse diaphragm muscle.

Antony, Claude; Huchet, Monique; Changeux, Jean‐Pierre; Cartaud, Jean

doi:10.1083/jcb.130.4.959

Cited by 19 publications

(11 citation statements)

References 45 publications

(63 reference statements)

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“…These proteins are in turn transported to their sites of action and CHC22 may have a role in these specific transport pathways. The process of innervation stimulates the localization of some proteins to NMJs and it can also influence membrane traffic at NMJs (Antony et al, 1995). The pattern of CHC22 distribution in regenerating muscle was consistent with its localization being controlled by innervation.…”

Section: Roles For Chc22 At Specialized Regions Of the Sarcolemmamentioning

confidence: 55%

Clathrin Isoform CHC22, a Component of Neuromuscular and Myotendinous Junctions, Binds Sorting Nexin 5 and Has Increased Expression during Myogenesis and Muscle Regeneration

Towler

Gleeson

Hoshino

et al. 2004

MBoC

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The muscle isoform of clathrin heavy chain, CHC22, has 85% sequence identity to the ubiquitously expressed CHC17, yet its expression pattern and function appear to be distinct from those of well-characterized clathrin-coated vesicles. In mature muscle CHC22 is preferentially concentrated at neuromuscular and myotendinous junctions, suggesting a role at sarcolemmal contacts with extracellular matrix. During myoblast differentiation, CHC22 expression is increased, initially localized with desmin and nestin and then preferentially segregated to the poles of fused myoblasts. CHC22 expression is also increased in regenerating muscle fibers with the same time course as embryonic myosin, indicating a role in muscle repair. CHC22 binds to sorting nexin 5 through a coiled-coil domain present in both partners, which is absent in CHC17 and coincides with the region on CHC17 that binds the regulatory light-chain subunit. These differential binding data suggest a mechanism for the distinct functions of CHC22 relative to CHC17 in membrane traffic during muscle development, repair, and at neuromuscular and myotendinous junctions.

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Section: Roles For Chc22 At Specialized Regions Of the Sarcolemmamentioning

confidence: 55%

Clathrin Isoform CHC22, a Component of Neuromuscular and Myotendinous Junctions, Binds Sorting Nexin 5 and Has Increased Expression during Myogenesis and Muscle Regeneration

Towler

Gleeson

Hoshino

et al. 2004

MBoC

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“…Thus, the production of NSIST by motor neurons could distinguish synaptic from extrasynaptic C S through differential sulfation, an interesting possibility given the view that the degree of sulfation of synaptic C S is probably important to its f unction (Mook-Jung and Gordon, 1995;Bowen et al, 1996). Although we did not observe elevated NSIST levels at neuromuscular junctions, it is noteworthy that a specialized Golgi apparatus exists just under the postsynaptic membrane (Ralston et al, 1993;Antony et al, 1995). It is thus feasible that NSIST is also selectively expressed at junctional nuclei in muscle.…”

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confidence: 43%

Expression Cloning and Characterization of NSIST, a Novel Sulfotransferase Expressed by a Subset of Neurons and Postsynaptic Targets

et al. 1998

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Synapses are distinguished by localized concentrations of specific proteins, many of which bear the marks of posttranslational processing such as glycosylation and sulfation. One strategy to elucidate this posttranslational tailoring is to identify the enzymes that create these modifications. Monoclonal antibody 3B3 recognizes a carbohydrate-containing epitope expressed on dystroglycan and other constituents of Torpedo electric organ synaptic membranes. We used mAb 3B3 in an immunofluorescence-based expression-cloning method and isolated a cDNA clone conferring mAb-3B3 immunoreactivity to transfected COS cells. The deduced polypeptide has a predicted molecular weight of 51 kDa, a type II transmembrane topology, and four potential N-linked glycosylation sites. The polypeptide, which we term NSIST (nervous system involved sulfotransferase), shows extensive, although not complete, homology to a chondroitin-6-sulfotransferase and limited homology to other sulfotransferases. In NSIST-transfected COS cells, 35 SO 4 incorporation and chondroitin-sulfate-like immunoreactivity are increased. In vivo, NSIST occurs as a single 2.4 kb transcript abundant in Torpedo electric organ, moderately expressed in spinal cord and electric lobe, and undetectable in non-neural tissues. Immunohistochemistry shows that NSIST is expressed in a punctate distribution in the innervated portion of electrocytes. In the CNS, NSIST-like immunoreactivity is localized within the somas of motor neurons and neurons of the electromotor nucleus, whereas mAb-3B3 immunostaining is associated with cell surfaces and neuropil. Neuronal NSIST is therefore likely to exert its effects extracellularly; although NSIST is synthesized by neurons, its product, the 3B3 epitope, is found outside neuronal cell bodies. Our evidence indicates that NSIST participates in nervous system specific posttranslational modifications, perhaps including those at synapses.

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“…Rough ER was previously visualized by electron microscopy in a continuum with the nuclear membrane, as one of a few morphologically-defined sites within adult rabbit cardiomyocytes [35]. Translation around myonuclei in cardiomyocytes for specific cardiac proteins has not been reported to our knowledge, but has been discussed as one of at least two such sites in skeletal muscle myocytes [36]. …”

Section: Discussionmentioning

confidence: 99%

Rough endoplasmic reticulum to junctional sarcoplasmic reticulum trafficking of calsequestrin in adult cardiomyocytes

McFarland

Milstein²,

Cala

2010

Journal of Molecular and Cellular Cardiology

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Cardiac calsequestrin (CSQ) is synthesized on rough endoplasmic reticulum (ER), but concentrates within the junctional sarcoplasmic reticulum (SR) lumen where it becomes part of the Ca 2+ -release protein complex. To investigate CSQ trafficking through biosynthetic/secretory compartments of adult cardiomyocytes, CSQ-DsRed was overexpressed in cultured cells and examined using confocal fluorescence microscopy. By 48 h of adenovirus treatment, CSQ-DsRed fluorescence had specifically accumulated in perinuclear cisternae, where it co-localized with markers of rough ER. From rough ER, CSQ-DsRed appeared to traffic directly to junctional SR along a transverse (Z-line) pathway along which sec 23-positive (ER-exit) sites were enriched. In contrast to DsRed direct fluorescence that presumably reflected DsRed tetramer formation, both anti-DsRed and anti-CSQ immunofluorescence did not detect the perinuclear CSQ-DsRed protein, but labeled only junctional SR puncta. These putative CSQ-DsRed monomers, but not the fluorescent tetramers, were observed to traffic anterogradely over the course of a 48 h overexpression from rough ER towards the cell periphery. We propose a new model of CSQ and junctional SR protein traffic in the adult cardiomyocyte, wherein CSQ traffics from perinuclear cisternae, along contiguous ER/SR lumens in cardiomyocytes as a mobile monomer, but is retained in junctional SR as a polymer.

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Developmental regulation of membrane traffic organization during synaptogenesis in mouse diaphragm muscle.

Cited by 19 publications

References 45 publications

Clathrin Isoform CHC22, a Component of Neuromuscular and Myotendinous Junctions, Binds Sorting Nexin 5 and Has Increased Expression during Myogenesis and Muscle Regeneration

Clathrin Isoform CHC22, a Component of Neuromuscular and Myotendinous Junctions, Binds Sorting Nexin 5 and Has Increased Expression during Myogenesis and Muscle Regeneration

Expression Cloning and Characterization of NSIST, a Novel Sulfotransferase Expressed by a Subset of Neurons and Postsynaptic Targets

Rough endoplasmic reticulum to junctional sarcoplasmic reticulum trafficking of calsequestrin in adult cardiomyocytes

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