It is highly important in Japan to choose a good site for wind turbine generators, because the spatial distribution of wind speed is quite complicated over steep complex terrain. We are developing the unsteady numerical model called the RIAM-COMPACT (Research Institute for Applied Mechanics, Kyushu University, Computational Prediction of Airflow over Complex Terrain). The RIAM-COMPACT is based ...

The membrane localization and activation of cytoskeletal protein talin are key steps to initiate the integrin transmembrane receptors' activation, which mediates many cellular adhesive responses such as cell migration, spreading and proliferation. RIAM, a membrane anchor and small GTPase RAP1 effector, is known to bind to the C-terminal rod domain of talin (talin-R) and promote localizations of...

It is highly important in Japan to choose a good site for wind turbines, because the spatial distribution of wind speed is quite complicated over steep complex terrain. We are developing the unsteady numerical model called the Research Institute for Applied Mechanics, Kyushu University, COMputational Prediction of Airflow over Complex Terrain (RIAM-COMPACT). The RIAMCOMPACT is based on the larg...

Talin is an integrin adaptor, which controls integrin activity in all hematopoietic cells. How intracellular signals promote talin binding to the integrin tail leading to integrin activation is still poorly understood, especially in leukocytes. In vitro studies identified an integrin activation complex whose formation is initiated by the interaction of active, guanosine triphosphate (GTP)-bound...

The Rap1-GTP interacting adapter protein (RIAM) is an important protein in Rap1-mediated integrin activation. By binding to both Rap1 GTPase and talin, RIAM recruits talin to the cell membrane, thus facilitating talin-dependent integrin activation. In this article, we studied the role of the RIAM Ras-association (RA) and pleckstrin-homology (PH) domains in the interaction with Rap1. We found th...

Adaptive immunity depends on lymphocyte adhesion that is mediated by the integrin lymphocyte functional antigen 1 (LFA-1). The small guanosine triphosphatase Rap1 regulates LFA-1 adhesiveness through one of its effectors, Rap1-interacting adapter molecule (RIAM). We show that RIAM was recruited to the lymphocyte plasma membrane (PM) through its Ras association (RA) and pleckstrin homology (PH) ...