Folding, trimerization, and transport are sequential events in the biogenesis of influenza virus hemagglutinin

@article{Copeland1988FoldingTA,
  title={Folding, trimerization, and transport are sequential events in the biogenesis of influenza virus hemagglutinin},
  author={Constance S. Copeland and Klaus Peter Zimmer and K R Wagner and Glenn A. Healey and Ira Mellman and Ari Helenius},
  journal={Cell},
  year={1988},
  volume={53},
  pages={197-209}
}
Results from several systems indicate that correct protein folding and subunit assembly correlate with the transport of membrane and secretory proteins from the endoplasmic reticulum (ER) to the Golgi complex. Because the site of oligomer assembly and its precise relationship to intracellular transport remain unclear, we have studied in detail the folding and trimerization of the influenza virus hemagglutinin (HA0) relative to its transport from ER to Golgi. Trimerization and transport were… Expand
Assembly, sorting, and exit of oligomeric proteins from the endoplasmic reticulum
  • P. Reddy, R. Corley
  • Biology, Medicine
  • BioEssays : news and reviews in molecular, cellular and developmental biology
  • 1998
TLDR
Different strategies to ensure that only properly folded proteins enter the secretory pathway are discussed and some of the unique problems they present for the ER quality control system are discussed. Expand
Oligomerization, transport, and Golgi retention of Punta Toro virus glycoproteins
TLDR
Investigation of the oligomerization and intracellular transport of the membrane glycoproteins of Punta Toro virus, a member of the Phlebovirus genus of the family Bunyaviridae, which is assembled by budding in the Golgi complex, finds that the majority of the G1 and G2 glyCoproteins are assembled into noncovalently linked G1-G2 heterodimers. Expand
Folding of influenza hemagglutinin in the endoplasmic reticulum
TLDR
The folding of influenza hemagglutinin in the ER was analyzed in tissue culture cells by following the formation of intrachain disulfides after short (1 min) radioactive pulses, and the efficiency of folding and subsequent trimerization was not dependent on the rate of translation, nor on temperature between 37 and 15 degrees C; however, the rates of folded and trimmederization decreased with decreasing temperature. Expand
Oligomerization and intracellular protein transport: dimerization of intestinal dipeptidylpeptidase IV occurs in the Golgi apparatus.
TLDR
It is concluded that dimerization of di peptidylpeptidase IV occurs in a late Golgi compartment and therefore cannot be a prerequisite for its export from the endoplasmic reticulum. Expand
Differential effects of mutations in three domains on folding, quaternary structure, and intracellular transport of vesicular stomatitis virus G protein
TLDR
The results suggest that the cytoplasmic domain of the wild-type protein may facilitate rapid, efficient transport from the ER, which can be easily affected or eliminated by tail mutations that do not detectably affect the ectodomain. Expand
Folding, assembly, and posttranslational modification of proteins within the lumen of the endoplasmic reticulum.
TLDR
The lumen of the endoplasmic reticulum (ER) is a protein-folding compartment and proteins destined for secretion enter the lumen unfolded and leave folded and active. Expand
Bunyavirus protein transport and assembly.
TLDR
It has become evident that bunyavirus glycoproteins expressed from cloned cDNAs are retained in the Golgi complex and thus behave similarly to resident proteins of the Gol Gi complex. Expand
Protein interactions during coronavirus assembly
TLDR
The bovine coronavirus (BCV) is used as a model to study interactions between the viral proteins in virus-infected cells that are important for coronav virus assembly, and oligomerization and/or conformational changes may be important for the S-M-HE protein complexes to form. Expand
Formation and intracellular transport of a heterodimeric viral spike protein complex
TLDR
The results show that these two viral glycoproteins have different maturation kinetics in the ER, due to the different rates by which these proteins fold and become competent to enter into heterodimeric complexes prior to exit from the ER. Expand
Defective assembly and intracellular transport of mutant paramyxovirus hemagglutinin-neuraminidase proteins containing altered cytoplasmic domains
TLDR
Data suggest that the HN cytoplasmic tail may function in the assembly of the final transport-competent oligomeric form of HN and that mutant HN molecules with seemingly properly folded ectodomains are retained in the endoplasmic reticulum by an as yet unidentified mechanism. Expand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 77 REFERENCES
Assembly of influenza hemagglutinin trimers and its role in intracellular transport
TLDR
Investigation of the kinetics and cellular location of the assembly reaction that results in HA0 trimerization suggested that formation of correctly folded quaternary structure constitutes a key event regulating the transport of the protein out of the endoplasmic reticulum. Expand
Monoclonal antibodies localize events in the folding, assembly, and intracellular transport of the influenza virus hemagglutinin glycoprotein
TLDR
It is found that the globular head of the HA folds into its mature conformation in the endoplasmic reticulum prior to the assembly of HA monomers into trimers, and newly formed trimers are sensitive to acid-induced conformational alterations associated with viral fusion activity. Expand
Role for adenosine triphosphate in regulating the assembly and transport of vesicular stomatitis virus G protein trimers
TLDR
The results indicate that oligomerization of G protein occurs in several steps, is sensitive to cellular ATP, and is required for transport from the ER. Expand
Differential effects of mutations in three domains on folding, quaternary structure, and intracellular transport of vesicular stomatitis virus G protein
TLDR
The results suggest that the cytoplasmic domain of the wild-type protein may facilitate rapid, efficient transport from the ER, which can be easily affected or eliminated by tail mutations that do not detectably affect the ectodomain. Expand
Expression of wild-type and mutant forms of influenza hemagglutinin: The role of folding in intracellular transport
TLDR
It is shown that folding and assembly of hemagglutinin monomers into trimeric structures takes approximately 7-10 min and is completed before the protein leaves the endoplasmic reticulum. Expand
ATP-coupled transport of vesicular stomatitis virus G protein. Functional boundaries of secretory compartments.
TLDR
The data suggest that ATP-sensitive steps punctuate transport of protein between compartmental boundaries of the secretory pathway, which is required for maximal rates of transport between Golgi compartments. Expand
Pre- and post-golgi vacuoles operate in the transport of semliki forest virus membrane glycoproteins to the cell surface
TLDR
The effect of reduced temperature on synchronized transport of SFV membrane proteins from the ER via the Golgi complex to the surface of BHK-21 cells revealed two membrane compartments where transport could be arrested, and it is proposed that membrane proteins enter the Gol Gi stack via tubular extensions of the pre-Golgi vacuolar elements which generate the GolGI cisternae. Expand
Posttranslational oligomerization and cooperative acid activation of mixed influenza hemagglutinin trimers
TLDR
The formation of mixed trimers in cells expressing two different HA gene products are analyzed to establish that the acid-induced conformational change involved in the membrane fusion activity of HA is a highly cooperative event. Expand
Exit of newly synthesized membrane proteins from the trans cisterna of the Golgi complex to the plasma membrane
TLDR
The results suggest that the trans cisterna was distinct from the endosome compartment and that the latter was not an obligatory station in the route taken by G protein to the cell surface. Expand
Oligomerization is essential for transport of vesicular stomatitis viral glycoprotein to the cell surface
TLDR
It is concluded that formation of an oligomer of G protein, probably a trimer, is necessary for G protein maturation. Expand
...
1
2
3
4
5
...