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First published online 7 March 2006
doi: 10.1242/jcs.02846

Journal of Cell Science 119, 1233-1243 (2006)
Published by The Company of Biologists 2006
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Research Article

ER-bound PTP1B is targeted to newly forming cell-matrix adhesions

Mariana V. Hernández1, Maria G. Davies Sala1, Janne Balsamo2, Jack Lilien2 and Carlos O. Arregui1,*

1 Instituto de Investigaciones Biotecnológicas, IIB-INTECH, Universidad de San Martín, 1650 San Martín, Buenos Aires, Argentina
2 Department of Biological Sciences, University of Iowa, Iowa City, IA 52242, USA

* Author for correspondence (e-mail: carregui{at}iib.unsam.edu.ar)

Accepted 14 December 2005

Here, we define the mechanism through which protein tyrosine phosphatase 1B (PTP1B) is targeted to cell-matrix adhesion sites. Green fluorescent protein (GFP)-labeled PTP1B bearing the substrate-trapping mutation D181A was found in punctate structures in lamellae. The puncta co-localized with focal adhesion kinase (FAK) and Src, and defined the distal tips of cell-matrix adhesion sites identified with paxillin and vinculin. PTP1B is largely associated with the external face of the endoplasmic reticulum (ER) and the puncta develop from ER projections over cell-matrix adhesion sites, a process dependent on microtubules. Deletion of the ER-targeting sequence resulted in cytosolic localization and altered the distribution of PTP1B at cell-matrix foci, whereas mutations disrupting interactions with Src homology 3 (SH3) domains, and the insulin and cadherin receptors had no effect. PTP1B recognizes substrates within forming adhesion foci as revealed by its preferential association with paxillin as opposed to zyxin-containing foci. Our results suggest that PTP1B targets to immature cell-matrix foci in newly forming lamellae by dynamic extensions of the ER and contributes to the maturation of these sites.

Key words: PTP1B tyrosine phosphatase, Cell-matrix adhesion, Endoplasmic reticulum, Integrin signaling, Microtubules


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