| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
J. Biol. Chem., Vol. 277, Issue 47, 45644-45654, November 22, 2002
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
From the Department of Cell and Developmental Biology, University
of North Carolina-Chapel Hill, Chapel Hill, North Carolina
27599
The focal adhesion kinase (FAK) and cell adhesion
kinase 
(CAK, PYK2, CADTK, RAFTK) are highly homologous FAK
family members, yet clearly have unique roles in the cell. Comparative
analyses of FAK and CAK have revealed intriguing differences in
their activities. These differences were investigated further through the characterization of a set of FAK/CAK chimeric kinases. CAK exhibited greater catalytic activity than FAK in vitro,
providing a molecular basis for differential substrate phosphorylation
by FAK and CAK in vivo. Furthermore, the N terminus may
regulate catalytic activity since chimeras containing the FAK N
terminus and CAK catalytic domain exhibited a striking high level of
catalytic activity and substrate phosphorylation. Unexpectedly, a
modulatory role for the N termini in subcellular localization was also
revealed. Chimeras containing the FAK N terminus and CAK C terminus
localized to focal adhesions, whereas chimeras containing the N and C
termini of CAK did not. Finally, prominent changes in cell
morphology were induced upon expression of chimeras containing the
CAK N terminus, which were not associated with apoptotic cell death, cell cycle progression delay, or changes in Rho activity. These results demonstrate novel regulatory roles for the N terminus of FAK
family kinases.
To whom correspondence should be addressed: Dept. of Cell and
Developmental Biology CB7090 University of North Carolina-Chapel Hill,
Chapel Hill, NC 27599. Tel.: 919-966-0391; Fax: 919-966-1856; E-mail:
crispy4@med.unc.edu.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  D. F. J. Ceccarelli, H. K. Song, F. Poy, M. D. Schaller, and M. J. Eck Crystal Structure of the FERM Domain of Focal Adhesion Kinase J. Biol. Chem., January 6, 2006; 281(1): 252 - 259. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 P. V. Usatyuk and V. Natarajan Regulation of reactive oxygen species-induced endothelial cell-cell and cell-matrix contacts by focal adhesion kinase and adherens junction proteins Am J Physiol Lung Cell Mol Physiol, December 1, 2005; 289(6): L999 - L1010. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
L. A. Cohen and J.-L. Guan Residues within the First Subdomain of the FERM-like Domain in Focal Adhesion Kinase Are Important in Its Regulation J. Biol. Chem., March 4, 2005; 280(9): 8197 - 8207. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. M. Dunty, V. Gabarra-Niecko, M. L. King, D. F. J. Ceccarelli, M. J. Eck, and M. D. Schaller FERM Domain Interaction Promotes FAK Signaling Mol. Cell. Biol., June 15, 2004; 24(12): 5353 - 5368. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
L. A. Cooper, T.-L. Shen, and J.-L. Guan Regulation of Focal Adhesion Kinase by Its Amino-Terminal Domain through an Autoinhibitory Interaction Mol. Cell. Biol., November 15, 2003; 23(22): 8030 - 8041. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. T. Parsons Focal adhesion kinase: the first ten years J. Cell Sci., April 15, 2003; 116(8): 1409 - 1416. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
R. A. Worthylake and K. Burridge RhoA and ROCK Promote Migration by Limiting Membrane Protrusions J. Biol. Chem., April 4, 2003; 278(15): 13578 - 13584. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |
