In silico modulation of apoptotic Bcl-2 proteins by mistletoe lectin-1: Functional consequences of protein modifications
✍ Scribed by Tasneem A. Khwaja; Tayyaba Wajahat; Ishtiaq Ahmad; Daniel C. Hoessli; Evelyne Walker-Nasir; Afshan Kaleem; Wajahat M. Qazi; Abdul R. Shakoori; Nasir-ud- Din
- Publisher
- John Wiley and Sons
- Year
- 2008
- Tongue
- English
- Weight
- 437 KB
- Volume
- 103
- Category
- Article
- ISSN
- 0730-2312
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✦ Synopsis
Abstract
The mistletoe lectin‐1 (ML‐1) modulates tumor cell apoptosis by triggering signaling cascades through the complex interplay of phosphorylation and O‐linked N‐acetylglucosamine (O‐GlcNAc) modification in pro‐ and anti‐apoptotic proteins. In particular, ML‐1 is predicted to induce dephosphorylation of Bcl‐2‐family proteins and their alternative O‐GlcNAc modification at specific, conserved Ser/Thr residues. The sites for phosphorylation and glycosylation were predicted and analyzed using Netphos 2.0 and YinOYang 1.2. The involvement of modified Ser/Thr, and among them the potential Yin Yang sites that may undergo both types of posttranslational modification, is proposed to mediate apoptosis modulation by ML‐1. J. Cell. Biochem. 103: 479–491, 2008. © 2007 Wiley‐Liss, Inc.