Cloning and sequence analysis of desmosomal glycoproteins 2 and 3 (desmocollins): cadherin-like desmosomal adhesion molecules with heterogeneous cytoplasmic domains.
Cloning and sequence analysis of desmosomal glycoproteins 2 and 3 (desmocollins): cadherin-like desmosomal adhesion molecules with heterogeneous cytoplasmic domains.
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DOI：
10.1083/jcb.113.2.381
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发表时间：
1991-04
期刊：
影响因子：
--
通讯作者：
Garrod DR
中科院分区：
文献类型：
--
作者：
Collins JE;Legan PK;Kenny TP;MacGarvie J;Holton JL;Garrod DR
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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影响因子：
64.8
作者：
DUSTIN, ML;SELVARAJ, P;SPRINGER, TA
通讯作者：
SPRINGER, TA
DOI：
10.1083/jcb.100.1.327
发表时间：
1985-01
期刊：
The Journal of cell biology
影响因子：
--
作者：
Boller K;Vestweber D;Kemler R
通讯作者：
Kemler R
DOI：
10.1073/pnas.85.8.2613
发表时间：
1988-04-01
影响因子：
11.1
作者：
GREEN, KJ;GOLDMAN, RD;CHISHOLM, RL
通讯作者：
CHISHOLM, RL
DOI：
10.1073/pnas.82.3.810
发表时间：
1985-01-01
影响因子：
11.1
作者：
GORBSKY, G;COHEN, SM;STEINBERG, MS
通讯作者：
STEINBERG, MS
影响因子：
7.8
作者：
BOLOGNA, M;ALLEN, R;DULBECCO, R
通讯作者：
DULBECCO, R