Chromosomal mapping of the structural gene coding for the mouse cell adhesion molecule uvomorulin.

Eistetter, Harald; Adolph, Sabine; Ringwald, Martin; Simon-Chazottes, Dominique; Schuh, Reinhard; Guénet, Jean-Louis; Kemler, Rolf

doi:10.1073/pnas.85.10.3489

Cited by 28 publications

(9 citation statements)

References 29 publications

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“…Our results are similar to those obtained in mouse (43), where a single L-CAM (uvomorulin) gene was mapped to chromosome 8 and a cDNA probe used in the in situ hybridization experiments had weak cross-reactivity with chromosome 10.…”

Section: Resultssupporting

confidence: 88%

Structure of the gene for the liver cell adhesion molecule, L-CAM.

Sorkin

Hemperly²,

Edelman³

et al. 1988

Proc. Natl. Acad. Sci. U.S.A.

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The liver cell adhesion molecule, L-CAM, mediates calcium-dependent cell-cell adhesion in early embryos and in nonneural epithelia in adult tissues. Earlier studies of cDNAs for chicken L-CAM established the amino acid sequence of the mature protein. The sequence has now been extended in the 5' direction through the precursor and signal sequences and past a consensus translation initiation site. The combined cDNAs were used to isolate genomic clones covering the entire L-CAM coding sequence. The structural gene for chicken L-CAM contains 16 exons ranging in size from 115 to over 1045 base pairs with an average size of 222 base pairs. Single exons do-not correspond to known structural elements such as. the signal sequence, precursor segment, internal repeats, or membrane-spanning region of L-CAM.

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Section: Resultssupporting

confidence: 88%

Structure of the gene for the liver cell adhesion molecule, L-CAM.

Sorkin

Hemperly²,

Edelman³

et al. 1988

Proc. Natl. Acad. Sci. U.S.A.

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“…The clustering of human cadherin genes on chromosome 16 has been well preserved in a highly syntenic region of mouse Chromosome 8. The mouse genes for E-cadherin (Cdh1; Eistetter et al, 1988), P-cadherin (Cdh3; Hatta et al, 1991), VE-cadherin (Cdh5; Huber et al, 1996), M-cadherin (Cdh15, Kaupmann et al, 1992), OB-cadherin (Cdh11; Hoffman and Balling, 1995), and now Ksp-cadherin (Cdh16) are all reported to be located within a region spanning 10 -25 cM of Chromosome 8. From an evolutionary standpoint, this clustering of cadherin genes suggests that most members of the cadherin superfamily arose by gene duplication from a single ancestral gene.…”

Section: Chromosomal Localization Of Human and Mouse Ksp-cadherinmentioning

confidence: 99%

cDNA Cloning and Chromosomal Localization of the Human and Mouse Isoforms of Ksp-Cadherin

et al. 1998

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“…Oligonucleotides complementary to uvomorulin cDNA sequences were synthesized (Applied Biosystems) and used as primers in dideoxynucleotide sequencing (9) of genomic clone UG4c (10). Complete exon and adjacent intron sequences were determined.…”

mentioning

confidence: 99%

Uvomorulin-catenin complex formation is regulated by a specific domain in the cytoplasmic region of the cell adhesion molecule.

Ozawa

Ringwald

Kemler

1990

Proc. Natl. Acad. Sci. U.S.A.

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We have recently found that the cytoplasmic region of the cell adhesion molecule uvomorulin associates with three proteins named catenin a, fi, and y. Here we show by analysis of various mutant uvomorulin polypeptides expressed in mouse L cells that this association is mediated by a specific domain in the cytoplasmic region. A specific recognition site for catenins is located in a 72-amino acid domain. Interestingly, 69 of the 72 amino acid residues are encoded by a single exon of the uvomorulin gene. To demonstrate the direct interaction between catenins and the 72-amino acid domain, cDNA constructs composed of H-2Kd cDNA and various 3' sequences of uvomorulin were expressed in L cells. Chimeric proteins between H-2Kd and the 72-amino acid domain of uvomorulin were shown, by immunoprecipitation with anti-H-2Kd antibodies, to complex with catenin a, (, and y. Catenins connect uvomorulin to cytoskeletal structures. We provide biochemical evidence for an association of the uvomorulin-catenin complex with actin bundles. Our results suggest that catenin a plays a key role in the association with actin filaments, whereas catenin (3 binds more directly to the cytoplasmic region of uvomorulin.In cell aggregation assays with transfected cells expressing normal or mutant uvomorulin, the adhesive function was expressed only when uvomorulin was associated with catenins. From these results we conclude that the cytoplasmic anchorage of uvomorulin is of major biological importance.

show abstract

Chromosomal mapping of the structural gene coding for the mouse cell adhesion molecule uvomorulin.

Cited by 28 publications

References 29 publications

Structure of the gene for the liver cell adhesion molecule, L-CAM.

Structure of the gene for the liver cell adhesion molecule, L-CAM.

cDNA Cloning and Chromosomal Localization of the Human and Mouse Isoforms of Ksp-Cadherin

Uvomorulin-catenin complex formation is regulated by a specific domain in the cytoplasmic region of the cell adhesion molecule.

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