Changes in HOXB6 homeodomain protein structure and localization during human epidermal development and differentiation
| Autor: | Eric Stelnicki, Angela Kwong, László G. Kömüves, Theadora Mauro, Anastasia Blink, Sophia Rozenfeld, Billy Y. B. Lau, Corey Largman, Wei-Fang Shen, Keerthi Krishnan, Yuko Oda |
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| Rok vydání: | 2000 |
| Předmět: |
Adult
Keratinocytes Cytoplasm Time Factors Transcription Genetic Recombinant Fusion Proteins EMX2 Biology Transfection DNA-binding protein NKX2-3 Protein structure Proto-Oncogene Proteins Humans RNA Messenger Hox gene Transcription factor Cells Cultured In Situ Hybridization Cell Nucleus Homeodomain Proteins Dose-Response Relationship Drug Reverse Transcriptase Polymerase Chain Reaction Pre-B-Cell Leukemia Transcription Factor 1 fungi Cell Differentiation Immunohistochemistry Molecular biology Protein subcellular localization prediction DNA-Binding Proteins Epidermal Cells embryonic structures Homeobox Calcium Epidermis Developmental Biology |
| Zdroj: | Developmental Dynamics. 218:636-647 |
| ISSN: | 1097-0177 1058-8388 |
| DOI: | 10.1002/1097-0177(2000)9999:9999<::aid-dvdy1014>3.0.co;2-i |
| Popis: | HOX homeodomain proteins are master developmental regulators, which are now thought to function as transcription factors by forming cooperative DNA binding complexes with PBX or other protein partners. Although PBX proteins exhibit regulated subcellular localization and function in the nucleus in other tissues, little data exists on HOX and PBX protein localization during skin development. We now show that the HOXB6 protein is expressed in the suprabasal layer of the early developing epidermis and throughout the upper layers of late fetal and adult human skin. HOXB6 signal is cytoplasmic throughout fetal epidermal development, but substantially nuclear in normal adult skin. HOXB6 protein is also partially nuclear in hyperproliferative skin conditions, but appears to be cytoplasmic in basal and squamous cell carcinomas. Although all three PBX genes are expressed in fetal epidermis, none of the three PBX proteins exhibit nuclear co-localization with HOXB6 in either fetal or adult epidermis. RNA and protein data suggest that a truncated HOXB6 protein, lacking the homeodomain, is expressed in undifferentiated keratinocytes and that the full-length protein is induced by differentiation. GFP-fusion proteins were used to demonstrate that the full-length HOXB6 protein is localized to the nucleus while the truncated protein is largely cytoplasmic. Taken together, these data suggest that during epidermal development the truncated HOXB6 isoform may function by a mechanism other than as DNA binding protein, and that most of the nuclear, homeodomain-containing HOXB6 protein does not utilize PBX proteins as DNA binding partners in the skin. Published 2000 Wiley-Liss, Inc. |
| Databáze: | OpenAIRE |
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