Regular ArticleIn VivoInteraction of AF-6 with Activated Ras and ZO-1☆
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2008, Neurobiology of DiseaseCitation Excerpt :7H6 (155 kDa) is a phosphoprotein that reversibly dissociates from the TJ under conditions of adenosine triphosphate (ATP) depletion, associated with increased paracellular permeability (Satoh et al., 1996; Zhong et al., 1994). The AF-6 (180 kDa) protein participates in the regulations of tight junctions, via direct interaction with ZO-1 (Yamamoto et al., 1999). To date, several other accessory proteins found in epithelial and peripheral endothelial cell TJs have been implicated as potential mediators of paracellular regulation (e.g. junction-associated coiled-coil protein (JACOP), calcium-dependent serine protein kinase (CASK), regulator of G-protein signaling-5 (RG-5)) (Hawkins and Davis, 2005; Zlokovic, 2008), yet confirmation of their existence or activity within BBB endothelial cells is presently lacking.
The cytoplasmic plaque of tight junctions: A scaffolding and signalling center
2008, Biochimica et Biophysica Acta - BiomembranesCitation Excerpt :Afadin contains one PDZ domain, which interacts with the C-termini of nectin and JAM Ig-like adhesion molecules, and the Eph subfamily of receptor tyrosine kinases [62–64]. The first Ras-binding domain within the N-terminus of afadin regulates the activity of the small GTPase Rap1 and interacts with Ras [65–67] (Fig. 1). The invertebrate homolog of afadin, Canoe, is thought to be an effector of Rap1 and both an effector and target of Ras in vivo [68–70].
The Cerebral Microcirculation
2008, Microcirculation
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Abbreviations used: RA domain, Ras-associating domain; N-terminal, amino-terminal; C-terminal, carboxyl-terminal; Raf-RBD, Ras-binding domain in Raf; RalGDS-RID, Ras-interacting domain in RalGDS; GST, glutathione-S-transferase; MBP, maltose-binding protein; DTT, dithiothreitol; IPTG, isopropyl-β-D-thiogalactoside; GTPγS, guanosine 5′-(3-O-thio)-triphosphate; DSP, dithiobis(succinimidylpropionate); RGL-RID, RGL (RalGDS like) Ras-interacting domain
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To whom correspondence should be addressed at Division of Signal Transduction, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0101, Japan. Fax: +81-743-72-5449. E-mail:[email protected].