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Cloning and sequence analysis of desmosomal glycoprotein 2 and 3 cDNAs: cadherin-like desmosomal adhesion molecules with heterogeneous cytoplasmic domains

Collins, J.E., Legan, P.K., Kenny, T.P., Macgarvie, J., Holton, J.L. and Garrod, D.R. (1991) Cloning and sequence analysis of desmosomal glycoprotein 2 and 3 cDNAs: cadherin-like desmosomal adhesion molecules with heterogeneous cytoplasmic domains PloS one, 113, (2), pp. 381-391. (doi:10.1083/jcb.113.2.381).

Record type: Article


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 lambda gt11 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 extracellular domain of dg3 shows 39.4% protein sequence identity with bovine N-cadherin and 28.4% identity with the other major desmosomal glycoprotein, dg1, or desmoglein. The cytoplasmic domain of dg3 and the partial cytoplasmic domain of dg2 show 23 and 24% identity with bovine N-cadherin, respectively. The results support our previous model for the transmembrane organization of dg2 and 3 (Parrish, E.P., J.E. Marston, D.L. Mattey, H.R. Measures, R. Venning, and D.R. Garrod. 1990. J. Cell Sci. 96:239-248; Holton, J.L., T.P. Kenny, P.K. Legan, J.E. Collins, J.N. Keen, R. Sharma, and D.R. Garrod. 1990. J. Cell Sci. 97:239-246). They suggest that these glycoproteins are specialized for calcium-dependent adhesion in their extracellular domains and, cytoplasmically, for the molecular interactions involved in desmosome plaque formation. Moreover this represents the first example of alternative splicing within the cadherin family of cell adhesion molecules.

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Published date: 15 April 1991
Organisations: Infection Inflammation & Immunity


Local EPrints ID: 179799
ISSN: 1932-6203
PURE UUID: d395b23e-9142-4d0d-8d88-a3fc566a8a00

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Date deposited: 07 Apr 2011 14:39
Last modified: 18 Jul 2017 12:02

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Author: J.E. Collins
Author: P.K. Legan
Author: T.P. Kenny
Author: J. Macgarvie
Author: J.L. Holton
Author: D.R. Garrod

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