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cDNA Cloning, Expression, and Assembly Characteristics of Mouse Keratin 16

Porter, R.M.; Hutcheson, A.M.; Rugg, E.L.; Quinlan, R.A.; Lane, E.B.

cDNA Cloning, Expression, and Assembly Characteristics of Mouse Keratin 16 Thumbnail


Authors

R.M. Porter

A.M. Hutcheson

E.L. Rugg

E.B. Lane



Abstract

There has been speculation as to the existence of the mouse equivalent of human type I keratin 16 (K16). The function of this keratin is particularly intriguing because, in normal epidermis, it is usually confined to hair follicles and only becomes expressed in the suprabasal intrafollicular regions when the epidermis is traumatized. Previous studies suggested that K16 is highly expressed in the skin of mice carrying a truncated K10 gene. We therefore used the skin of heterozygous and homozygous mice to create a cDNA library, and we report here the successful cloning and sequencing of mouse K16. Recent in vitro studies suggested that filaments formed by human K16 are shorter than those formed by other type I keratins. One hypothesis put forward was that a proline residue in the 1B subdomain of the helical domain was responsible. The data presented here demonstrate that this proline is not conserved between mouse and human, casting doubt on the proposed function of this proline residue in filament assembly. In vitro assembly studies showed that mouse K16 produced long filaments in vitro. Also, in contrast to previous observations, transfection studies of PtK2 cells showed that mouse K16 (without the proline) and also human K16 (with the proline) can incorporate into the endogenous K8/K18 network without detrimental effect. In addition, K16 from both species can form filaments de novo when transfected with human K5 into immortalized human lens epithelial cells, which do not express keratins. These results suggest that reduced assembly capabilities due to unusual sequence characteristics in helix 1B are not the key to the unique function of K16. Rather, these data implicate the tail domain of K16 as the more likely protein domain that determines the unique functions.

Citation

Porter, R., Hutcheson, A., Rugg, E., Quinlan, R., & Lane, E. (1998). cDNA Cloning, Expression, and Assembly Characteristics of Mouse Keratin 16. Journal of Biological Chemistry, 273(48), 32265-32272. https://doi.org/10.1074/jbc.273.48.32265

Journal Article Type Article
Online Publication Date Nov 27, 1998
Publication Date Nov 27, 1998
Deposit Date Dec 20, 2017
Publicly Available Date Mar 28, 2024
Journal Journal of Biological Chemistry
Print ISSN 0021-9258
Electronic ISSN 1083-351X
Publisher American Society for Biochemistry and Molecular Biology
Peer Reviewed Peer Reviewed
Volume 273
Issue 48
Pages 32265-32272
DOI https://doi.org/10.1074/jbc.273.48.32265

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Copyright Statement
This research was originally published in The Journal of Biological Chemistry. Rebecca M. Porter, Alene M. Hutcheson, Elizabeth L. Rugg, Roy A. Quinlan and E. Birgitte Lane. cDNA Cloning, Expression, and Assembly Characteristics of Mouse Keratin 16. The Journal of Biological Chemistry. 1998. 273: 32265-32272. © the American Society for Biochemistry and Molecular Biology





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