当前位置： SCI文献检索 > BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS期刊下所有文献 > The focal adhesion kinase amino-terminal domain localises to nuclei and intercellular junctions in HEK 293 and MDCK cells independently of tyrosine 397 and the carboxy-terminal domain.

The focal adhesion kinase amino-terminal domain localises to nuclei and intercellular junctions in HEK 293 and MDCK cells independently of tyrosine 397 and the carboxy-terminal domain.

Abstract：

:The function and intracellular localisation of the non-catalytic NH(2)-terminal region of focal adhesion kinase (FAK) are unclear. We investigated the targetting of the FAK NH(2)-terminal domain in HEK 293 and epithelial MDCK cells. Exogenous expression of a variety of GFP-fused and epitope-tagged NH(2) terminal domain constructs either including or lacking the major Tyr 397 autophosphorylation and Src-binding site targeted to nuclei and cell-cell junctions in HEK 293 cells and co-localised at junctions with occludin, and beta1 integrin subunits at junctions. Mutation of Tyr 397 also had no effect on localisation of the NH(2)-terminal domain. In contrast, constructs encoding either the kinase or focal adhesion targeting (FAT) domains but lacking the NH(2)-terminal region failed to localise to intercellular junctions or nuclei. The NH(2)-terminal domain was not associated with beta1 integrin subunits as indicated by co-immunoprecipitation experiments, but did co-localise with cortical actin filaments. The NH(2)-terminal domain also targetted to nuclei and intercellular junctions in MDCK cells, whereas full-length FAK localised only to focal adhesions in these cells. These results indicate that the FAK NH(2)-terminal domain targets to epithelial intercellular junctions and nuclei and suggest novel functions for FAK NH(2)-terminal domain fragments independent of Y397, kinase, and FAT domains.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Stewart A,Ham C,Zachary I

doi

10.1016/s0006-291x(02)02547-0

subject

Has Abstract

pub_date

2002-11-22 00:00:00

pages

62-73

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006291X02025470

journal_volume

299

pub_type

杂志文章

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