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In silico modulation of apoptotic Bcl-2 proteins by mistletoe lectin-1: functional consequences of protein modifications

Khwaja, Tasneem A.
Wajahat, Tayyaba
Ahmad, Ishtiaq
Walker-Nasir, Evelyne
Kaleem, Afshan
Qazi, Wajahat M.
Shakoori, Abdul R.
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Published in Journal of Cellular Biochemistry. 2008, vol. 103, no. 2, p. 479-91
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.
Keywords Amino Acid SequenceAnimalsApoptosis/drug effectsCatsCattleConserved SequenceCricetinaeCricetulusDeerDogsGlycosylation/drug effectsHumansMiceMolecular Sequence DataPhosphorylation/drug effectsPlant Preparations/pharmacologyPlant Proteins/pharmacologyProtein Processing, Post-Translational/drug effectsProto-Oncogene Proteins c-bcl-2/chemistry/drug effects/physiologyRibosome Inactivating Proteins, Type 2/pharmacologySequence AlignmentSheepSpecies SpecificityToxins, Biological/pharmacologyBcl-2-Associated X Protein/chemistry/drug effects/physiologyBcl-Associated Death Protein/chemistry/drug effects/physiology
PMID: 17583555
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KHWAJA, Tasneem A. et al. In silico modulation of apoptotic Bcl-2 proteins by mistletoe lectin-1: functional consequences of protein modifications. In: Journal of cellular biochemistry, 2008, vol. 103, n° 2, p. 479-91. doi: 10.1002/jcb.21412 https://archive-ouverte.unige.ch/unige:2489

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Deposited on : 2009-08-25

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