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Direct binding of RalA to PKCη and its crucial role in morphological change during keratinocyte differentiation.
- Source :
-
Molecular biology of the cell [Mol Biol Cell] 2011 Apr 15; Vol. 22 (8), pp. 1340-52. Date of Electronic Publication: 2011 Feb 23. - Publication Year :
- 2011
-
Abstract
- During differentiation, keratinocytes undergo a dramatic shape change from small and round to large and flat, in addition to production of proteins necessary for the formation of epidermis. It has been shown that protein kinase C (PKC) η is crucial for keratinocyte differentiation. However, its role in this process has yet to be fully elucidated. Here, we show that catalytic activity is not necessary for enlarged and flattened morphology of human keratinocytes induced by overexpression of PKCη, although it is important for gene expression of the marker proteins. In addition, we identify the small G protein RalA as a binding partner of PKCη, which binds to the C1 domain, an indispensable region for the morphological change. The binding led activation of RalA and actin depolymerization associated with keratinocyte differentiation. siRNA techniques proved that RalA is involved in not only the keratinocyte differentiation induced by PKCη overexpression but also normal keratinocyte differentiation induced by calcium and cholesterol sulfate. These results provide a new insight into the molecular mechanism of cytoskeletal regulation leading to drastic change of cell shape.
- Subjects :
- Actins metabolism
Adenoviridae
Binding Sites
Calcium metabolism
Calcium pharmacology
Cell Shape drug effects
Cholesterol Esters pharmacology
Enzyme Activation
Epidermal Cells
Epidermis enzymology
Escherichia coli
Gene Expression physiology
Gene Silencing
HEK293 Cells
Humans
Mutation
Protein Binding physiology
Protein Kinase C genetics
Protein Structure, Tertiary
RNA, Small Interfering metabolism
Recombinant Proteins genetics
Transfection
ral GTP-Binding Proteins genetics
Cell Differentiation drug effects
Keratinocytes cytology
Keratinocytes enzymology
Protein Kinase C metabolism
Recombinant Proteins metabolism
ral GTP-Binding Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1939-4586
- Volume :
- 22
- Issue :
- 8
- Database :
- MEDLINE
- Journal :
- Molecular biology of the cell
- Publication Type :
- Academic Journal
- Accession number :
- 21346190
- Full Text :
- https://doi.org/10.1091/mbc.E10-09-0754