The fully linked HTML version of this article has now been published.
JCS ePress
online publication date 18 Oct 2005
doi: 10.1242/jcs.02620
Research Article
NOSTRIN functions as a homotrimeric adaptor protein facilitating internalization of eNOS
Ann Icking,
Simone Matt,
Nils Opitz,
Anja Wiesenthal,
Werner Müller-Esterl*,
and
Kirstin Schilling
* Author for correspondence (e-mail: wme{at}biochem2.de)
Intracellular trafficking of endothelial nitric oxide synthase (eNOS) between different compartments is incompletely understood. Recently, we described a novel eNOS-interacting protein, NOSTRIN, which upon overexpression drives eNOS away from the plasma membrane towards intracellular compartments. Sequence similarity of NOSTRIN and pacsins/syndapins suggested a role for NOSTRIN in endocytosis. Accordingly, we show here that NOSTRIN interacts with the large GTPase dynamin and the actin nucleation promoting factor N-WASP by means of its SH3 domain, which also represents the docking site for eNOS. Via a coiled-coil region in the C-terminal portion of the protein, NOSTRIN oligomerizes, mainly forming trimers, which would allow simultaneous interaction with multiple binding partners of the SH3 domain. Consistent with this notion, expression of dynamin-2-GFP in CHO cells stably expressing eNOS (CHO-eNOS) results in recruitment of eNOS to dynamin-positive structures, only when NOSTRIN is present as well. Similarly, when N-WASP-GFP and NOSTRIN are co-expressed in CHO-eNOS cells, both proteins strongly co-localize with eNOS and are recruited to structures running along actin filaments. If, however, the actin cytoskeleton is depolymerized by cytochalasin D, NOSTRIN and eNOS are associated with extended structures in the cell periphery, possibly being unable to leave the plasma membrane. Together, these results indicate that NOSTRIN may facilitate endocytosis of eNOS by coordinating the function of dynamin and N-WASP.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati 
Twitter What's this?
This article has been cited by other articles:
|
|
|
|
 
S. M. Hartig, S. Ishikura, R. S. Hicklen, Y. Feng, E. G. Blanchard, K. A. Voelker, C. S. Pichot, R. W. Grange, R. M. Raphael, A. Klip, et al.
The F-BAR protein CIP4 promotes GLUT4 endocytosis through bidirectional interactions with N-WASp and Dynamin-2
J. Cell Sci.,
July 1, 2009;
122(13):
2283 - 2291.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
D. M. Dudzinski and T. Michel
Life history of eNOS: Partners and pathways
Cardiovasc Res,
July 15, 2007;
75(2):
247 - 260.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
S. Mukhopadhyay, F. Xu, and P. B. Sehgal
Aberrant cytoplasmic sequestration of eNOS in endothelial cells after monocrotaline, hypoxia, and senescence: live-cell caveolar and cytoplasmic NO imaging
Am J Physiol Heart Circ Physiol,
March 1, 2007;
292(3):
H1373 - H1389.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
N. Kang-Decker, S. Cao, S. Chatterjee, J. Yao, L. J. Egan, D. Semela, D. Mukhopadhyay, and V. Shah
Nitric oxide promotes endothelial cell survival signaling through S-nitrosylation and activation of dynamin-2
J. Cell Sci.,
February 1, 2007;
120(3):
492 - 501.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
K. Schilling, N. Opitz, A. Wiesenthal, S. Oess, R. Tikkanen, W. Muller-Esterl, and A. Icking
Translocation of Endothelial Nitric-Oxide Synthase Involves a Ternary Complex with Caveolin-1 and NOSTRIN
Mol. Biol. Cell,
September 1, 2006;
17(9):
3870 - 3880.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
S. Mukherjee, M. Tessema, and A. Wandinger-Ness
Vesicular Trafficking of Tyrosine Kinase Receptors and Associated Proteins in the Regulation of Signaling and Vascular Function
Circ. Res.,
March 31, 2006;
98(6):
743 - 756.
[Abstract]
[Full Text]
[PDF]
|
|
|
© The Company of Biologists Ltd 2005
