First published online October 27, 2005
Journal of Cell Science 118, 2103e (2005)
© The Company of Biologists Limited
NO way out of the membrane
The control of blood flow is an important biological function of nitric oxide (NO). The production of NO in blood vessels by endothelial NO synthase (eNOS) causes the surrounding smooth muscle to relax. The activity of eNOS depends on its subcellular localization and, on p. 5059, Werner Müller-Esterl and colleagues report that eNOS trafficking inducer (NOSTRIN) can facilitate the movement of eNOS from the plasma membrane to intracellular vesicles and thereby attenuate its activity. NOSTRIN has sequence similarity to pacsin/syndapin - an endocytic effector protein that interacts with both the large GTPase dynamin, which is involved in endocytic vesicle formation, and the neural Wiskott-Aldrich syndrome protein (N-WASP), which helps form the actin tails that propel vesicles through the cytoplasm. The authors show that NOSTRIN, like pacsin/syndapin, interacts with dynamin and N-WASP through its SH3 domain, which is also the docking site for eNOS. Other data indicate that trimerization of NOSTRIN allows it to interact simultaneously with eNOS, N-WASP and dynamin. Thus, by coordinating dynamin and N-WASP function, NOSTRIN may facilitate endocytosis of eNOS and dampen production of NO.
Related articles in JCS:
- 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
JCS 2005 118: 5059-5069.
[Abstract]
[Full Text]
