| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
J Biol Chem, Vol. 274, Issue 31, 21515-21518, July 30, 1999
From the Department of Medicine, University of Pennsylvania,
Philadelphia, Pennsylvania 19104
We have identified a cDNA for pleckstrin 2 that is 39% identical and 65% homologous to the original pleckstrin.
Like the original pleckstrin 1, this protein contains a pleckstrin
homology (PH) domain at each end of the molecule as well as a DEP
(Dishevelled, Egl-10, and
pleckstrin) domain in the intervening sequence. A Northern
blot probed with the full-length cDNA reveals that this homolog is
ubiquitously expressed and is most abundant in the thymus, large bowel,
small bowel, stomach, and prostate. Unlike pleckstrin 1, this newly
discovered protein does not contain obvious sites of PKC
phosphorylation, and in transfected Cos-7 cells, it is a poor substrate
for phosphorylation, even after PMA stimulation. Cells
expressing pleckstrin 2 undergo a dramatic shape change associated with
actin rearrangement, including a loss of central F-actin and a
redistribution of actin toward the cell cortex. Overexpression of
pleckstrin 2 causes large lamellipodia and peripheral ruffle formation.
A variant of pleckstrin 2 lacking both PH domains still had some
membrane binding but did not efficiently induce lamellipodia,
suggesting that the PH domains of pleckstrin 2 contribute to
lamellipodia formation. This work describes a novel, widely expressed,
membrane-associating protein and suggests that pleckstrin 2 may help
orchestrate cytoskeletal arrangement.
This article has been cited by other articles:
|
|
 |
|
  T. L. Bach, W. T. Kerr, Y. Wang, E. M. Bauman, P. Kine, E. L. Whiteman, R. S. Morgan, E. K. Williamson, E. M. Ostap, J. K. Burkhardt, et al. PI3K regulates pleckstrin-2 in T-cell cytoskeletal reorganization Blood, February 1, 2007; 109(3): 1147 - 1155. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 B. A. Buckley, A. Y. Gracey, and G. N. Somero The cellular response to heat stress in the goby Gillichthys mirabilis: a cDNA microarray and protein-level analysis J. Exp. Biol., July 15, 2006; 209(14): 2660 - 2677. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. Komatsu, K. Hiyama, K. Tanimoto, M. Yunokawa, K. Otani, M. Ohtaki, E. Hiyama, J. Kigawa, M. Ohwada, M. Suzuki, et al. Prediction of individual response to platinum/paclitaxel combination using novel marker genes in ovarian cancers. Mol. Cancer Ther., March 1, 2006; 5(3): 767 - 775. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. E. Williams, J. Torabinejad, E. Cohick, K. Parker, E. J. Drake, J. E. Thompson, M. Hortter, and D. B. DeWald Mutations in the Arabidopsis Phosphoinositide Phosphatase Gene SAC9 Lead to Overaccumulation of PtdIns(4,5)P2 and Constitutive Expression of the Stress-Response Pathway Plant Physiology, June 1, 2005; 138(2): 686 - 700. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 W. Ning, T. J. Chu, C. J. Li, A. M. K. Choi, and D. G. Peters Genome-wide analysis of the endothelial transcriptome under short-term chronic hypoxia Physiol Genomics, June 17, 2004; 18(1): 70 - 78. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 G. S. Bogatkevich, E. Tourkina, C. S. Abrams, R. A. Harley, R. M. Silver, and A. Ludwicka-Bradley Contractile activity and smooth muscle {alpha}-actin organization in thrombin-induced human lung myofibroblasts Am J Physiol Lung Cell Mol Physiol, August 1, 2003; 285(2): L334 - L343. [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 |
