Inhibition of acetylcholine receptor assembly by activity in primary cultures of embryonic rat muscle cells.

Carlin, B E; Lawrence, John C.; Lindstrom, Jon; Merlie, John P.

doi:10.1016/s0021-9258(19)89231-1

Cited by 26 publications

(13 citation statements)

References 29 publications

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“…Some independent event could, in principle, initiate both assembly and transport. Several reports in other systems have, however, indicated that subunit assembly may be a key factor in allowing transport of proteins to the plasma membrane (3,10,21,22). Subunits of some newly synthesized plasma membrane and secretory proteins are known to remain in the ER if the appropriate subunits or co-factors are not available.…”

Section: The Role Of Quaternary Structure In Transportmentioning

confidence: 99%

“…The early change is detected by an increase in the affinity of the alpha subunit for a ligand, bungarotoxin. The second change involves a stable association between the alpha-and beta-subunits in velocity sedimentation experiments, and it may regulate surface delivery of the receptor (10). Cases in which quaternary interactions seem to play an important role in regulating efficiency of transport and sorting are also known in the endocytic pathway.…”

Section: The Role Of Quaternary Structure In Transportmentioning

confidence: 99%

“…In this case assembly is thought to occur in the endoplasmic reticulum (ER) 1 or in the Golgi complex (1,6,30,36,39,41,53). Several reports have suggested that subunit assembly is important in the regulation of membrane protein transport in the secretory pathway (6,10,28,41,42,55), but little is yet known about the assembly events at the molecular level.…”

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confidence: 99%

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Assembly of influenza hemagglutinin trimers and its role in intracellular transport.

Copeland¹,

Doms²,

Bolzau³

et al. 1986

The Journal of Cell Biology

396

343

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Abstract. The hemagglutinin (HA) of influenza virus is a homotrimeric integral membrane glycoprotein. It is cotranslationally inserted into the endoplasmic reticulum as a precursor called HA0 and transported to the cell surface via the Golgi complex. We have, in this study, investigated the kinetics and cellular location of the assembly reaction that results in HA0 trimerization. Three independent criteria were used for determining the formation of quaternary structure: the appearance of an epitope recognized by trimer-specific monoclonal antibodies; the acquisition of trypsin resistance, a characteristic of trimers; and the formation of stable complexes which cosedimented with the mature HA0 trimer (9S20.w) in sucrose gradients containing Triton X-100.The results showed that oligomer formation is a posttranslational event, occurring with a half time of ~7.5 min after completion of synthesis. Assembly occurs in the endoplasmic reticulum, followed almost immediately by transport to the Golgi complex. A stabilization event in trimer structure occurs when HA0 leaves the Golgi complex or reaches the plasma membrane. Approximately 10% of the newly synthesized HA0 formed aberrant trimers which were not transported from the endoplasmic reticulum to the Golgi complex or the plasma membrane. Taken together the results suggested that formation of correctly folded quaternary structure constitutes a key event regulating the transport of the protein out of the endoplasmic reticulum. Further changes in subunit interactions occur as the trimers move along the secretory pathway.

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Section: The Role Of Quaternary Structure In Transportmentioning

confidence: 99%

Section: The Role Of Quaternary Structure In Transportmentioning

confidence: 99%

See 1 more Smart Citation

Assembly of influenza hemagglutinin trimers and its role in intracellular transport.

Copeland¹,

Doms²,

Bolzau³

et al. 1986

The Journal of Cell Biology

396

343

View full text Add to dashboard Cite

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“…In these cells, a 2.2 + 0.2-fold increase in c~-subunit protein was determined aftertreatment with ascorbic acid. This increase in the ~ cells is somewhat lower than is seen in the surface AChR and may indicate that further regulation occurs in the assembly and insertion of this protein (a phenomenon also reported for rat primary cells in response to muscle inactivity by Carlin et al, 1986).…”

Section: Synthesis Of Tr-subunit Protein Does Not Increase In Response To Ascorbic Acidmentioning

confidence: 72%

“…In light of our current results, it would be interesting to evaluate whether some regulation at the level of translation may not also contribute to the control of surface receptor expression in response to neural factors in chick cells. Similarly, it is interesting that after inactivation of muscle activity by tetrodotoxin, the increases in a-mRNA exceed or equal those in surface receptors (Klarsfeld and Changeux, 1985;Harris et al, 1988) while the increase in u-subunit synthesis is not as great as that in surface receptor (Carlin et al, 1986). Although the differences in these studies could be due to species differences (the mRNA studies having been performed in chick cells and the protein studies in rat cells), the possibility is raised that some of the regulation of surface AChR by muscle activity may also be at the level of translation.…”

Section: Discussionmentioning

confidence: 99%

Regulation of acetylcholine receptor synthesis at the level of translation in rat primary muscle cells.

Horovitz

Spitsberg

Salpeter

1989

The Journal of Cell Biology

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Abstract. Previous studies have shown that rat primary muscle cells do not respond to crude rat brain extract or one of its active components, ascorbic acid, with a significant increase in surface acetylcholine receptor (AChR) number. We report here that, although little or no response is seen on the cell surface, rat primary muscle cells do respond to both crude brain extract and to ascorbic acid with an approximately threefold increase in AChR o~-subunit mRNA. The response of the mRNA is similar to that seen in the cloned L5 cells. However, while in L5 cells the increase in ot-subunit mRNA is further translated into increased levels of ot-subunit protein, there is no such increase in a-subunit synthesis in the primary cells. This study thus shows a regulation of surface AChR synthesis in rat primary cells at the level of ot-subunit translation. This level of regulation is different from that involving subunit transcription or subunit assembly reported by others.

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Regulation of the number of α‐bungarotoxin binding sites in cultured chick myotubes by a 1,4 dihydropyridine calcium channel antagonist

Smilowitz¹,

Smart²,

Bowik³

et al. 1988

J of Neuroscience Research

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Calcium has been suggested as the second messenger link between skeletal muscle activity and AChR gene expression and synthesis. We have compared the concentrations of the Ca2+ channel antagonists D600 and nisoldipine needed both to block Ca2+ uptake into cultured myotubes and to increase AChR expression. The good correspondence between these two measurements and the use of the highly specific Ca2+ channel antagonist nisoldipine strengthens the hypothesis that AChR expression is regulated by levels of intracellular Ca2+.

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Inhibition of acetylcholine receptor assembly by activity in primary cultures of embryonic rat muscle cells.

Cited by 26 publications

References 29 publications

Assembly of influenza hemagglutinin trimers and its role in intracellular transport.

Assembly of influenza hemagglutinin trimers and its role in intracellular transport.

Regulation of acetylcholine receptor synthesis at the level of translation in rat primary muscle cells.

Regulation of the number of α‐bungarotoxin binding sites in cultured chick myotubes by a 1,4 dihydropyridine calcium channel antagonist

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