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Molecular and Cellular Biology, January 2004, p. 154-163, Vol. 24, No. 1
0270-7306/04/$08.00+0     DOI: 10.1128/MCB.24.1.154-163.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Assessment of Splice Variant-Specific Functions of Desmocollin 1 in the Skin

Xing Cheng,1,2 Kusal Mihindukulasuriya,2 Zhining Den,2 Andrew P. Kowalczyk,3 Cathárine C. Calkins,3 Akira Ishiko,4 Atsushi Shimizu,4 and Peter J. Koch1,2*

Departments of Molecular and Cellular Biology,1 Dermatology, Baylor College of Medicine, Houston, Texas,2 Department of Dermatology, Emory University, Atlanta, Georgia,3 Department of Dermatology, Keio University School of Medicine, 35 Shinanomachi, Shinjuku, Tokyo, Japan4

Received 26 February 2003/ Returned for modification 28 April 2003/ Accepted 9 October 2003

Desmocollin 1 (Dsc1) is part of a desmosomal cell adhesion receptor formed in terminally differentiating keratinocytes of stratified epithelia. The dsc1 gene encodes two proteins (Dsc1a and Dsc1b) that differ only with respect to their COOH-terminal cytoplasmic amino acid sequences. On the basis of in vitro experiments, it is thought that the Dsc1a variant is essential for assembly of the desmosomal plaque, a structure that connects desmosomes to the intermediate filament cytoskeleton of epithelial cells. We have generated mice that synthesize a truncated Dsc1 receptor that lacks both the Dsc1a- and Dsc1b-specific COOH-terminal domains. This mutant transmembrane receptor, which does not bind the common desmosomal plaque proteins plakoglobin and plakophilin 1, is integrated into functional desmosomes. Interestingly, our mutant mice did not show the epidermal fragility previously observed in dsc1-null mice. This suggests that neither the Dsc1a- nor the Dsc1b-specific COOH-terminal cytoplasmic domain is required for establishing and maintaining desmosomal adhesion. However, a comparison of our mutants with dsc1-null mice suggests that the Dsc1 extracellular domain is necessary to maintain structural integrity of the skin.

* Corresponding author. Mailing address: Department of Molecular and Cellular Biology, Room S701, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030. Phone: (713) 798-3308. Fax: (713) 798-3800. E-mail: pkoch{at}bcm.tmc.edu.

Molecular and Cellular Biology, January 2004, p. 154-163, Vol. 24, No. 1
0022-538X/04/$08.00+0     DOI: 10.1128/MCB.24.1.154-163.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Chen, J., Den, Z., Koch, P. J. (2008). Loss of desmocollin 3 in mice leads to epidermal blistering. J. Cell Sci. 121: 2844-2849 [Abstract] [Full Text]  
  • Chen, J., Cheng, X., Merched-Sauvage, M., Caulin, C., Roop, D. R., Koch, P. J. (2006). An unexpected role for keratin 10 end domains in susceptibility to skin cancer. J. Cell Sci. 119: 5067-5076 [Abstract] [Full Text]  
  • Den, Z., Cheng, X., Merched-Sauvage, M., Koch, P. J. (2006). Desmocollin 3 is required for pre-implantation development of the mouse embryo. J. Cell Sci. 119: 482-489 [Abstract] [Full Text]  
  • Hardman, M. J., Liu, K., Avilion, A. A., Merritt, A., Brennan, K., Garrod, D. R., Byrne, C. (2005). Desmosomal Cadherin Misexpression Alters {beta}-Catenin Stability and Epidermal Differentiation. Mol. Cell. Biol. 25: 969-978 [Abstract] [Full Text]  
  • Yang, T., Liang, D., Koch, P. J., Hohl, D., Kheradmand, F., Overbeek, P. A. (2004). Epidermal detachment, desmosomal dissociation, and destabilization of corneodesmosin in Spink5-/- mice. Genes Dev. 18: 2354-2358 [Abstract] [Full Text]  


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