|
|
 Previous Article | Table of Contents | Next Article 
Blood, 1 May 2001, Vol. 97, No. 9, pp. 2633-2639
HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
CrkL is an adapter for Wiskott-Aldrich syndrome protein
and Syk
Atsushi Oda,
Hans D. Ochs,
Laurence A. Lasky,
Susan Spencer,
Katsutoshi Ozaki,
Mitsuhiro Fujihara,
Makoto Handa,
Kenji Ikebuchi, and
Hisami Ikeda
From the Hokkaido Red Cross Blood Center, Sapporo, and
the Department of Medicine and Blood Center, Keio University, Tokyo,
Japan; the Department of Pediatrics, University of Washington, School
of Medicine, Seattle, WA; and the Department of Molecular Oncology,
Genentech, San Francisco, CA.
Wiskott-Aldrich syndrome (WAS) and X-linked thrombocytopenia are
caused by mutations of the WAS protein (WASP) gene. WASP may be
involved in the regulation of podosome, an actin-rich dynamic cell
adhesion structure formed by various types of cells. The molecular
links between WASP and podosomes or other cell adhesion structures are
unknown. Platelets express an SH2-SH3 adapter molecule, CrkL, that can
directly associate with paxillin, which is localized in podosomes. The
hypothesis that CrkL binds to WASP was, therefore, tested. Results from
coprecipitation experiments using anti-CrkL and GST-fusion proteins
suggest that CrkL binds to WASP through its SH3 domain and that the
binding was not affected by WASP tyrosine phosphorylation. The binding
of GST-fusion SH3 domain of PSTPIP1 in vitro was also not affected by
WASP tyrosine phosphorylation, suggesting that the binding of the SH3
domains to WASP is not inhibited by tyrosine phosphorylation of WASP.
Anti-CrkL also coprecipitates a 72-kd protein, which was identified as
syk tyrosine kinase, critical for collagen induced-platelet activation.
CrkL immunoprecipitates contain kinase-active syk, as evidenced by an
in vitro kinase assay. Coprecipitation experiments using GST-fusion CrkL proteins suggest that both SH2 and SH3 domains of CrkL are involved in the binding of CrkL to syk. WASP, CrkL, syk, and
paxillin-like Hic-5 incorporated to platelet cytoskeleton after
platelet aggregation. Thus, CrkL is a novel molecular adapter for WASP
and syk and may potentially transfer these molecules to the
cytoskeleton through association with cytoskeletal proteins such as
Hic-5.
 CiteULike  Connotea  Del.icio.us  Digg  Reddit  Technorati What's this?
This article has been cited by other articles:
|
|
|
|
 
H. Falet, M. P. Marchetti, K. M. Hoffmeister, M. J. Massaad, R. S. Geha, and J. H. Hartwig
Platelet-associated IgAs and impaired GPVI responses in platelets lacking WIP
Blood,
November 19, 2009;
114(21):
4729 - 4737.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
H K Datta, W F Ng, J A Walker, S P Tuck, and S S Varanasi
The cell biology of bone metabolism
J. Clin. Pathol.,
May 1, 2008;
61(5):
577 - 587.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
S. Tsuboi and J. Meerloo
Wiskott-Aldrich Syndrome Protein Is a Key Regulator of the Phagocytic Cup Formation in Macrophages
J. Biol. Chem.,
November 23, 2007;
282(47):
34194 - 34203.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
J. H. Lee, Y. M. Kim, N. W. Kim, J. W. Kim, E. Her, B. K. Kim, J. H. Kim, S. H. Ryu, J. W. Park, D. W. Seo, et al.
Phospholipase D2 acts as an essential adaptor protein in the activation of Syk in antigen-stimulated mast cells
Blood,
August 1, 2006;
108(3):
956 - 964.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
Y. Calle, N. O. Carragher, A. J. Thrasher, and G. E. Jones
Inhibition of calpain stabilises podosomes and impairs dendritic cell motility
J. Cell Sci.,
June 1, 2006;
119(11):
2375 - 2385.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
J.-C. Gevrey, B. M. Isaac, and D. Cox
Syk Is Required for Monocyte/Macrophage Chemotaxis to CX3CL1 (Fractalkine)
J. Immunol.,
September 15, 2005;
175(6):
3737 - 3745.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
A. Oda, H. Miki, I. Wada, H. Yamaguchi, D. Yamazaki, S. Suetsugu, M. Nakajima, A. Nakayama, K. Okawa, H. Miyazaki, et al.
WAVE/Scars in platelets
Blood,
April 15, 2005;
105(8):
3141 - 3148.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
K. D. Moon, C. B. Post, D. L. Durden, Q. Zhou, P. De, M. L. Harrison, and R. L. Geahlen
Molecular Basis for a Direct Interaction between the Syk Protein-tyrosine Kinase and Phosphoinositide 3-Kinase
J. Biol. Chem.,
January 14, 2005;
280(2):
1543 - 1551.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
Y. Calle, G. E. Jones, C. Jagger, K. Fuller, M. P. Blundell, J. Chow, T. Chambers, and A. J. Thrasher
WASp deficiency in mice results in failure to form osteoclast sealing zones and defects in bone resorption
Blood,
May 1, 2004;
103(9):
3552 - 3561.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
A. Kettner, L. Kumar, I. M. Anton, Y. Sasahara, M. de la Fuente, V. I. Pivniouk, H. Falet, J. H. Hartwig, and R. S. Geha
WIP Regulates Signaling via the High Affinity Receptor for Immunoglobulin E in Mast Cells
J. Exp. Med.,
February 2, 2004;
199(3):
357 - 368.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
T. Yuminamochi, Y. Yatomi, M. Osada, T. Ohmori, Y. Ishii, K. Nakazawa, S. Hosogaya, and Y. Ozaki
Expression of the LIM Proteins Paxillin and Hic-5 in Human Tissues
J. Histochem. Cytochem.,
April 1, 2003;
51(4):
513 - 522.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
A. Oda, I. Wada, K. Miura, K. Okawa, T. Kadoya, T. Kato, H. Nishihara, M. Maeda, S. Tanaka, K. Nagashima, et al.
CrkL Directs ASAP1 to Peripheral Focal Adhesions
J. Biol. Chem.,
February 14, 2003;
278(8):
6456 - 6460.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
H. Nishihara, M. Maeda, A. Oda, M. Tsuda, H. Sawa, K. Nagashima, and S. Tanaka
DOCK2 associates with CrkL and regulates Rac1 in human leukemia cell lines
Blood,
December 1, 2002;
100(12):
3968 - 3974.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
