Premium
In silico modulation of apoptotic Bcl‐2 proteins by mistletoe lectin‐1: Functional consequences of protein modifications
Author(s) -
Khwaja Tasneem A.,
Wajahat Tayyaba,
Ahmad Ishtiaq,
Hoessli Daniel C.,
WalkerNasir Evelyne,
Kaleem Afshan,
Qazi Wajahat M.,
Shakoori Abdul R.,
Din Nasirud
Publication year - 2007
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.21412
Subject(s) - phosphorylation , apoptosis , dephosphorylation , lectin , glycosylation , microbiology and biotechnology , glycoprotein , protein phosphorylation , chemistry , biology , signal transduction , biochemistry , phosphatase , protein kinase a
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.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom