The immunoglobulin μ chains of membrane-bound and secreted IgM molecules differ in their C-terminal segments

Kehry, Marilyn R.; Ewald, Sandra J.; Douglas, R.; Sibley, Carol Hopkins; Raschke, William C.; Fambrough, Douglas M.; Hood, Leroy

doi:10.1016/0092-8674(80)90476-6

Cited by 150 publications

(53 citation statements)

References 41 publications

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“…Many cellular and viral transmembrane proteins, such as the erythrocyte glycophorin (27,231,40), heavy chains of membrane-associated IgM (234,108) and the histocompatibility antigens (249,160), as well as the envelope glycoprotein (G protein) of VSV (106) have their amino-terminal ends exposed on the luminal or extracellular face of membranes and the carboxy-terminal portions on the cytoplasmic side. It may be postulated that all proteins of this transmembrane disposition are synthesized in membrane-bound ribosomes and that their orientation results from cotranslational insertion of the polypeptides into the membrane by a process akin to an interrupted vectorial discharge (Fig; 1).…”

Section: The Disposition Of a Protein In A Membrane As A Results Of Thmentioning

confidence: 99%

“…Recent studies have indicated that membrane-associated and secretory IgM contain 1L-chains that differ in peptide segments located at their extreme carboxy-terminal ends (108,206,234). Comparison of sequences of cDNA clones obtained from the mRNA of a single myeloma tumor revealed the existence of two types of messenger RNA for tL chains, which differed only in nucleotide sequences at their 3'-terminal ends (174) .…”

Section: Halt or Stop Transfer Signalsmentioning

confidence: 99%

See 1 more Smart Citation

Mechanisms for the incorporation of proteins in membranes and organelles.

Sabatini¹,

Kreibich²,

Morimoto³

et al. 1982

The Journal of Cell Biology

869

281

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Section: The Disposition Of a Protein In A Membrane As A Results Of Thmentioning

confidence: 99%

Section: Halt or Stop Transfer Signalsmentioning

confidence: 99%

Mechanisms for the incorporation of proteins in membranes and organelles.

Sabatini¹,

Kreibich²,

Morimoto³

et al. 1982

The Journal of Cell Biology

869

281

View full text Add to dashboard Cite

“…5). Despite m being 22 residues longer than s (36), the presence of an additional N-glycan in the s carboxyl-terminal tailpiece makes it difficult to distinguish the two chains electrophoretically (Fig. 5A, lane 1).…”

Section: Tcr␣ and Chains Present In Covalent Complexesmentioning

confidence: 99%

Reduction of Interchain Disulfide Bonds Precedes the Dislocation of Ig-µ Chains from the Endoplasmic Reticulum to the Cytosol for Proteasomal Degradation

Fagioli¹,

Mezghrani²,

Sitia³

2001

Journal of Biological Chemistry

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Proteins that fail to fold or assemble in the endoplasmic reticulum (ER) are generally dislocated across the membrane to be degraded by cytosolic proteasomes. To investigate how the quality control machinery handles individual subunits that are part of covalent oligomers, we have analyzed the fate of transport-competent Ig light (L) chains that form disulfide bonds with shortlived heavy chains. When expressed alone, L chains are secreted. In cells producing excess , most L chains are retained in the ER as covalent ⅐L or 2 ⅐L 2 complexes. While chains present in these complexes are degraded by proteasomes, L chains are stable. Few L chains are secreted; most reassociate with newly synthesized chains. Therefore, interchain disulfide bonds are reduced in the ER lumen before the dislocation of chains in a site from which freed L chains can be rapidly reinserted in the assembly line. The ER can thus sustain the simultaneous formation and reduction of disulfide bonds.

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“…At least two types of cellular transmembrane surface glycoproteins have very short cytoplasmic domains consisting of three amino acid residues, immunoglobulin ~ and 5 membrane heavy chains (#m, 5m) (11,25). From previous studies it was determined that biosynthesis and maturation of.//m or 5m occurs via a pathway similar to the VSV G protein: from the rough ER through the Golgi complex to the plasma membrane (53, 60).…”

mentioning

confidence: 99%

Cytoplasmic domains of cellular and viral integral membrane proteins substitute for the cytoplasmic domain of the vesicular stomatitis virus glycoprotein in transport to the plasma membrane.

Puddington¹,

Machamer²,

Rose³

1986

The Journal of Cell Biology

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Abstract. Oligonucleotide-directed mutagenesis was used to construct chimeric cDNAs that encode the extracellular and transmembrane domains of the vesicular stomatitis virus glycoprotein (G) linked to the cytoplasmic domain of either the immunoglobulin u membrane heavy chain, the hemagglutinin glycoprotein of influenza virus, or the small glycoprotein (023) of infectious bronchitis virus. Biochemical analyses and immunofluorescence microscopy demonstrated that these hybrid genes were correctly expressed in eukaryotic cells and that the hybrid proteins were transported to the plasma membrane. The rate of transport to the Golgi complex of G protein with an immunoglobulin # membrane cytoplasmic domain was approximately sixfold slower than G protein with its normal cytoplasmic domain. However, this rate was virtually identical to the rate of transport of ~m heavy chain molecules measured in the B cell line WEHI 231. The rate of transport of G protein with a hemagglutinin cytoplasmic domain was threefold slower than wild type G protein and G protein with a p23 cytoplasmic domain, which were transported at similar rates. The combined results underscore the importance of the amino acid sequence in the cytoplasmic domain for efficient transport of G protein to the cell surface. Also, normal cytoplasmic domains from other transmembrane glycoproteins can substitute for the G protein cytoplasmic domain in transport of G protein to the plasma membrane. The method of constructing precise hybrid proteins described here will be useful in defining functions of specific domains of viral and cellular integral membrane proteins.

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The immunoglobulin μ chains of membrane-bound and secreted IgM molecules differ in their C-terminal segments

Cited by 150 publications

References 41 publications

Mechanisms for the incorporation of proteins in membranes and organelles.

Mechanisms for the incorporation of proteins in membranes and organelles.

Reduction of Interchain Disulfide Bonds Precedes the Dislocation of Ig-µ Chains from the Endoplasmic Reticulum to the Cytosol for Proteasomal Degradation

Cytoplasmic domains of cellular and viral integral membrane proteins substitute for the cytoplasmic domain of the vesicular stomatitis virus glycoprotein in transport to the plasma membrane.

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