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Cited by 400

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Identification of sequences required for the efficient localization of the focal adhesion kinase, pp125FAK, to cellular focal adhesions.

Open access
Hildebrand, J D, Schaller, M D, Parsons, J T·1993·The Journal of cell biology

Abstract

The integrin family of heterodimeric cell surface receptors play critical roles in multiple biological processes by mediating cellular adhesion to the extracellular matrix (ECM). Adhesion triggers intracellular signaling cascades, including tyrosine phosphorylation and elevation of [Ca2+]i. The Focal Adhesion Kinase (FAK or pp125FAK), a protein tyrosine kinase that colocalizes with integrins in cellular focal adhesions, is a prime candidate for a mediator of integrin signaling events. Here we report an analysis of the domain structure of FAK in which we have identified a contiguous stretch of 159 amino acids within the COOH terminus essential for correct subcellular localization. When placed in the context of an unrelated cytosolic protein, this Focal Adhesion Targeting (FAT) sequence functions to efficiently mediate the focal adhesion localization of this fusion protein. Furthermore, this analysis suggests that pp125FAK cannot be activated oncogenically by mutation. This result could be explained if pp125FK either exhibits a narrow substrate specificity or is diametrically opposed by cellular phosphatases or other cellular processes.

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Crossref · 10.1083/jcb.123.4.993

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Metadata

Authors
Hildebrand, J. D., Schaller, M. D., & Parsons, J. T.
Venue
The Journal of cell biology
Published
1993-11-15
Volume
123
Issue
4
Pages
993-1005
ISSN
  • 0021-9525 (ISSN-L)
  • 1540-8140
OpenAlex
W2000983089
Cited by
400
References
1
FWCI
8.79
Type
journal article
Language
en
Open access
green

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