1. Volume 73, Issue 5, Pages 524-526 (March 2008)
Nephrin AKTs on actin: The slit diaphragm–actin cytoskeleton signaling network expands 
J. Schlondorff 
Kidney International 
Volume 73, Issue 5, Pages (March 2008)
DOI: /sj.ki
Copyright © 2008 International Society of Nephrology Terms and Conditions

2. Figure 1
The nephrin–actin network. (a) A subset of interactions through which nephrin is proposed to be linked to the actin cytoskeleton. Nephrin is shown in the unphosphorylated state. However, the effect of phosphorylation on most of the interactions depicted here has not been reported. (b) Nephrin interactions in response to tyrosine phosphorylation, such as can be mediated by Fyn. The in vivo signals regulating nephrin phosphorylation remain obscure. Phosphoinositide 3-kinase (PI3K) binding depends on Y1152 of rat nephrin, whereas Y1204 and Y1228 (and Y1191 in mice) lie within Nck SH2 binding consensus sequences. PI3K activation leads to an increase in PIP3 at the inner leaflet, recruiting various PH domain-containing proteins, including Akt and Rac guanine-nucleotide exchange factors. In the case of downstream effects of Akt and Rac activation, arrows are not meant to imply a direct effect. Please see Faul et al.4 for additional network connections between the actin cytoskeleton and slit diaphragm proteins other than nephrin. Synpo, synaptopodin.
Kidney International  , DOI: ( /sj.ki )
Copyright © 2008 International Society of Nephrology Terms and Conditions