Protein 4.1R regulates cell adhesion, spreading, migration and motility of mouse keratinocytes by modulating surface expression of β1 integrin | Zendy

Lixiang Chen | Zendy; Richard AC Hughes | Zendy; Anthony J. Baines | Zendy; John G. Conboy | Zendy; Narla Mohandas | Zendy; Xiuli An | Zendy

Open Access

Protein 4.1R regulates cell adhesion, spreading, migration and motility of mouse keratinocytes by modulating surface expression of β1 integrin

Author(s) -

Lixiang Chen,

Richard AC Hughes,

Anthony J. Baines,

John G. Conboy,

Narla Mohandas,

Xiuli An

Publication year - 2011

Publication title -

journal of cell science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.384

H-Index - 278

eISSN - 1477-9137

pISSN - 0021-9533

DOI - 10.1242/jcs.078170

Subject(s) - microbiology and biotechnology , biology , integrin , fibronectin , focal adhesion , motility , transmembrane protein , cytoskeleton , cell migration , cell adhesion , signal transducing adaptor protein , actin cytoskeleton , actin , keratinocyte , adhesion , cell , extracellular matrix , signal transduction , in vitro , biochemistry , receptor , chemistry , organic chemistry

Protein 4.1R is a membrane-cytoskeleton adaptor protein that has diverse roles in controlling the cell surface expression and/or function of transmembrane proteins, and in organizing F-actin. 4.1R is expressed in keratinocytes, but its role in these cells has not been explored. Here, we have investigated the role of 4.1R in skin using 4.1R(-/-) mice. Cell adhesion, spreading, migration and motility were significantly impaired in 4.1R(-/-) keratinocytes, and 4.1R(-/-) mice exhibited defective epidermal wound healing. Cultured 4.1R(-/-) keratinocytes on fibronectin failed to form actin stress fibres and focal adhesions. Furthermore, in the absence of 4.1R, the surface expression, and consequently the activity of β1 integrin were reduced. These data enabled the identification of a functional role for protein 4.1R in keratinocytes by modulating the surface expression of β1 integrin, possibly through a direct association between 4.1R and β1 integrin.

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