The Immunoglobulin Superfamily: Domains For Cell Surface Recognition

Williams, Alan F.

doi:10.1146/annurev.immunol.6.1.381

Cited by 304 publications

(348 citation statements)

References 49 publications

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“…The formation of disulfide bonds is important for the folding and stability of many proteins, particularly those exposed to the extracellular environment, such as MHC class I molecules. The importance of disulfide bonds is evident by their conservation, not only among MHC molecules, but also throughout members of the immunoglobulin superfamily (41). At present, 6048 Ig domains have been documented (http://smart.embl-heidelberg.de a ).…”

Section: Discussionmentioning

confidence: 99%

ER60/ERp57 forms disulfide‐bonded intermediates with MHC class I heavy chain

Lindquist¹,

Hämmerling

Trowsdale³

2001

FASEB j.

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We demonstrated previously that ER60/ERp57 is recruited into early folding intermediates in the MHC class I assembly pathway (1). ER60 binding preceded the binding of β‐2‐microglobulin and was dependent on the presence of properly trimmed oligosaccharide moieties on the class I heavy chain (HC). Hence, this interaction could not be temporally differentiated from that of calnexin. Here, we show that calnexin is required for the recruitment of ER60 into early folding complexes with the HC and that in the absence of calnexin, ER60 is replaced by another member of the thiol‐reductase family, ERp72. We demonstrate that once recruited, ER60 associates covalently with HC via a disulfide bond. The ER60/HC complexes were also found in late assembly complexes, noncovalently bound to the transporter associated with antigen processing and accounted for approximately one‐third of the ER60 associated with the transporter associated with antigen processing. These results demonstrate that ER60 assists in the creation of conserved disulfide bonds within the class I HC through the formation of a mixed disulfide intermediate.

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Section: Discussionmentioning

confidence: 99%

ER60/ERp57 forms disulfide‐bonded intermediates with MHC class I heavy chain

Lindquist¹,

Hämmerling

Trowsdale³

2001

FASEB j.

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“…Analyses of a wide variety of protein sequences have identified modules or cassettes, 40-100 amino acids, which appear to have evolved for specific proteidprotein interactions [19]. Among the best characterized of these modules are the Ig motifs defining the Ig superfamily [20]. Most members of this family are extracellular or cell-surface proteins, often involved in cell adhesion [201. Recently, a group of intracellular myosin-associated proteins have been identified in both vertebrate and invertebrate muscles which contain Ig C2 motifs [21].…”

mentioning

confidence: 99%

Complete sequence of human fast‐type and slow‐type muscle myosin‐binding‐protein C (MyBP‐C)

Weber

Vaughan

Reinach

et al. 1993

European Journal of Biochemistry

117

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Myosin‐binding‐protein C (MyBP‐C) is a myosin‐associated protein of unknown function found in the cross‐bridge‐bearing zone (C region) of A bands in striated muscle. Using a cDNA clone encoding the fast‐type isoform of chicken MyBP‐C, we screened a human fetal muscle cDNA library and isolated clones encoding the full‐length human fast‐type isoform of MyBP‐C. cDNA clones encoding the slow‐type isoform of human MyBP‐C, were also isolated and fully sequenced. Northern‐blot analysis demonstrated skeletal muscle‐specific expression of these gene products. Using human/hamster somatic‐cell hybrids, we were able to map the slow‐type MyBP‐C to human chromosome 12, and the fast‐type MyBP‐C to chromosome 19. The cDNA for human fast‐type MyBP‐C encodes a polypeptide of 1142 amino acids with an expected molecular mass of 128.1 kDa. Comparison of this cDNA with other members of the MyBP family reveals extensive primary‐sequence conservation. Each MyBP‐C contains seven immunoglobulin C2 motifs and three fibronectin type‐III repeats in the arrangement C2‐C2‐C2‐C2‐C2‐III‐III‐C2‐III‐C2. Regions of high identity shared by the chicken and the two human proteins are not restricted to the immunoglobulin and fibronectin motifs. Sequence comparison of all three proteins has allowed us to map a highly conserved region between the first and second C2 motifs, the only large spacer sequence present between motifs in these proteins.

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“…Restriction sites used for the reporter gene constructs are shown. (Lai et al, 1987) and Po (Filbin et al, 1990;Schneider-Schaulies et al, 1990), as well as the Ig domains of the immunoglobulins (Williams and Barclay, 1988). Likewise, both interrupted and non-interrupted modules encoding the F'NIII domains of rat fibronectin are found (Schwarzbauer et al, 1987).…”

Section: Discussionmentioning

confidence: 92%

The Gene of Chicken Axonin-1. Complete Structure and Analysis of the Promoter

et al. 1995

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We have isolated and characterised the gene encoding the chicken axonal cell adhesion molecule axonin-1. This gene comprises 23 exons distributed over approximately 40 kb. Each of the six immunoglobulin-like domains and the four fibronectin-type-III-like domains of axonin-1 is encoded by two exons. The introns between two domains are exclusively phase I. Their exon/intron borders correspond to the domain borders of the protein, suggesting that the gene of axonin-1 had been generated by exon shuffling. Three transcripts with a length of 4.3 kb, 5 kb, and 8 kb are found, and we provide evidence that they result from alternative use of polyadenylation signals. In situ hybridization revealed co-localisation of these transcripts in time and space in the developing chicken retina. Several identical transcription initiation sites were found in retina, brain, and cerebellum by RNase protection assay and anchored polymerase chain reaction. By transfection of HeLa cells, rat PC-12 phaeochromocytoma cells, and chicken embryonic fibroblasts with serially truncated segments of the 5'-flanking region linked to a luciferase reporter gene, we have found that the sequence from -91 to +56 relative to the transcription initiation site is sufficient to promote efficient gene expression. Tissue-specific expression of the axonin-1 gene seems to be regulated in part by sequences more than 1 kb upstream of the transcription initiation site. As revealed by computer analysis, the sequence immediately upstream of exon 1 contains an AP-2 binding site, a tumor phorbol-ester-responsive element, and a homeodomain protein binding site, but no canonical TATA box. A second AP-2 binding site and a homeodomain protein binding site are located within exon 1.

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The Immunoglobulin Superfamily: Domains For Cell Surface Recognition

Cited by 304 publications

References 49 publications

ER60/ERp57 forms disulfide‐bonded intermediates with MHC class I heavy chain

ER60/ERp57 forms disulfide‐bonded intermediates with MHC class I heavy chain

Complete sequence of human fast‐type and slow‐type muscle myosin‐binding‐protein C (MyBP‐C)

The Gene of Chicken Axonin-1. Complete Structure and Analysis of the Promoter

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