Pin-Pointing a New DAP Kinase Function: The Peptidyl-Proly Isomerase Pin1 Is Negatively Regulated by DAP Kinase-Mediated Phosphorylation  Shani Bialik, Adi Kimchi  Molecular Cell  Volume 42, Issue 2, Pages 139-141 (April 2011) DOI: 10.1016/j.molcel.2011.04.002 Copyright © 2011 Elsevier Inc. Terms and Conditions

Figure 1 Molecular Pathways Triggered by DAPK (A) DAPK signaling network. DAPK has several distinct target proteins, each of which mediates the various functional arms of the kinase. Direct targets are depicted by polygons, indirect targets by ovals. Known substrates are indicated with a P for phosphorylation. Note that DAPK activates MARK1/2 independently of phosphorylation. (B) The DAPK/Pin1 connection. DAPK phosphorylates Pin1, thereby inhibiting its isomerase activity. Solid arrows lead to the functions and cellular outcomes of Pin1 that have been shown to be affected by DAPK, while dashed arrows lead to those that are postulated to be relevant to DAPK signaling, but not yet proven. MT, microtubules. Molecular Cell 2011 42, 139-141DOI: (10.1016/j.molcel.2011.04.002) Copyright © 2011 Elsevier Inc. Terms and Conditions