Identification of a cadherin cell adhesion recognition sequence

Blaschuk, Orest W.; Sullivan, Robert; David, Samuel; Pouliot, Yannick

doi:10.1016/0012-1606(90)90290-y

Cited by 365 publications

(206 citation statements)

References 16 publications

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“…Furthermore, these fragments and even small decapeptides containing the HAV sequence, known to be involved in homophilic recognition, can disturb proper cell-cell adhesion (Blaschuk et al, 1990). Therefore, it may be interesting to investigate the treatment of lobular tumours with related antibodies that can be synthesized in vitro according to the genes with truncation or splice site mutations.…”

Section: Discussionmentioning

confidence: 99%

Chromosome alterations and E-cadherin gene mutations in human lobular breast cancer

et al. 1999

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We have studied a set of 40 human lobular breast cancers for loss of heterozygosity (LOH) at various chromosome locations and for mutations in the coding region plus flanking intron sequences of the E-cadherin gene. We found a high frequency of LOH (100%, 31/31) at 16q21–q22.1. A significantly higher level of LOH was detected in ductal breast tumours at chromosome arms 1p, 3p, 9p, 11q, 13q and 18q compared to lobular breast tumours. Furthermore, we found a significant association between LOH at 16 q containing the E-cadherin locus and lobular histological type. Six different somatic mutations were detected in the E-cadherin gene, of which three were insertions, two deletions and one splice site mutation. Mutations were found in combination with LOH of the wild type E-cadherin locus and loss of or reduced E-cadherin expression detected by immunohistochemistry. The mutations described here have not previously been reported. We compared LOH at different chromosome regions with E-cadherin gene mutations and found a significant association between LOH at 13 q and E-cadherin gene mutations. A significant association was also detected between LOH at 13q and LOH at 7q and 11q. Moreover, we found a significant association between LOH at 3 p and high S phase, LOH at 9p and low ER and PgR content, LOH at 17p and aneuploidy. We conclude that LOH at 16q is the most frequent chromosome alteration and E-cadherin is a typical tumour suppressor gene in lobular breast cancer. © 1999 Cancer Research Campaign

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Section: Discussionmentioning

confidence: 99%

Chromosome alterations and E-cadherin gene mutations in human lobular breast cancer

et al. 1999

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“…EC1 was first modeled as the adhesive domain because it was found to be involved in specificity, contained the HAV adhesion sequence, and N-cadherin EC1 packed in an antiparallel orientation as if in a trans-dimer in one crystal form (Blaschuk et al 1990;Nose et al 1990;Shapiro et al 1995). However, the precise orientation of EC1 in the trans-dimer remains unclear.…”

Section: Further Functional Studies Of Ec Domains In Adhesionmentioning

confidence: 99%

Cadherin Adhesion: Mechanisms and Molecular Interactions

Perez

Nelson

2004

Handbook of Experimental Pharmacology

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Cadherins constitute a superfamily of cell-cell adhesion molecules expressed in many different cell types that are required for proper cellular function and maintenance of tissue architecture. Classical cadherins are the best understood class of cadherins. They are single membrane spanning proteins with a divergent extracellular domain of five repeats and a conserved cytoplasmic domain. Binding between cadherin extracellular domains is weak, but strong cell-cell adhesion develops during lateral clustering of cadherins by proteins that link the cadherin cytoplasmic domain to the actin cytoskeleton. Understanding how different regions of cadherins regulate cellcell adhesion has been a major focus of study. Here, we examine evidence of the structure and function of the extracellular domain of classical cadherins in regard to the control of recognition and adhesive contacts between cadherins on opposing cell surfaces. Early experiments that focused on understanding the homotypic, Ca ++ -dependent characteristics of cadherin adhesion are discussed, and data supporting the widely accepted cis-and trans-dimer models of cadherins are analyzed.

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“…Adhesive binding in the cadherins is believed to involve the amino acid triplet HAV (Fig. 5) (Blaschuk et al, 1990;Nose et al, 1990). The corresponding sequence in dg3 is YAT and in dgl is RAL.…”

Section: Discussionmentioning

confidence: 99%

“…Within the dg3 molecule the greatest identity is between EC2 and EC4 (30.4%) and the least is between EC1 and EC3 (14.4%). (d) The HAY adhesion sequence of N-cad (Blaschuk et al, 1990;Nose et al, 1990) is represented by YAT in dg3 and RAL in dgl (boxed in Fig. 5).…”

Section: Sequence Homologies With Cadherins and Dglmentioning

confidence: 99%

Cloning and sequence analysis of desmosomal glycoproteins 2 and 3 (desmocollins): cadherin-like desmosomal adhesion molecules with heterogeneous cytoplasmic domains.

Collins

Legan

Kenny

et al. 1991

The Journal of Cell Biology

183

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Abstract. Desmosomal glycoproteins 2 and 3 (dg2 and 3) or desmocollins have been implicated in desmosome adhesion. We have obtained a 5.0-kb-long clone for dg3 from a bovine nasal epidermal hgtl 1 cDNA library. Sequence analysis of this clone reveals an open reading frame of 2,517 bases encoding a polypeptide of 839 amino acids. The sequence consists of a signal peptide of 28 amino acids, a precursor sequence of 104 amino acids, and a mature protein of 707 amino acids. The latter has the characteristics of a transmembrane glycoprotein with an extracellular domain of 550 amino acids and a cytoplasmic domain of 122 amino acids.The sequence of a partial clone from the same library shows that dg2 has an alternative COOH terminus that is extended by 54 amino acids. Genomic DNA sequence data show that this arises by splicing out of a 46-bp exon that encodes the COOH-terminal 11 amino acids of dg3 and contains an in-frame stop codon.The extraceUular domain of dg3 shows 39.4% protein sequence identity with bovine N-cadherin and 28.4% identity with the other major desmosomal glycoprotein, dgl, or desmoglein. The cytoplasmic domain of dg3 and the partial cytoplasmic domain of rig2 show 23 and 24% identity with bovine N-cadherin, respectively.The results support our previous model for the transmembrane organization of dg2 and

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Identification of a cadherin cell adhesion recognition sequence

Cited by 365 publications

References 16 publications

Chromosome alterations and E-cadherin gene mutations in human lobular breast cancer

Chromosome alterations and E-cadherin gene mutations in human lobular breast cancer

Cadherin Adhesion: Mechanisms and Molecular Interactions

Cloning and sequence analysis of desmosomal glycoproteins 2 and 3 (desmocollins): cadherin-like desmosomal adhesion molecules with heterogeneous cytoplasmic domains.

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