Publication Name	World Journal of Biological Chemistry
Manuscript ID	21390
Country	United States

Received	2015-07-09 08:38
Peer-Review Started	2015-07-14 10:31
To Make the First Decision	2015-10-08 16:07
Return for Revision	2015-10-13 14:25
Revised	2015-10-16 05:23
Second Decision	2015-11-27 15:57
Accepted by Journal Editor-in-Chief	2015-11-29 12:55
Accepted by Executive Editor-in-Chief	2015-12-08 15:18
Articles in Press	2015-12-08 15:18
Publication Fee Transferred
Edit the Manuscript by Language Editor
Typeset the Manuscript	2016-02-19 11:45
Publish the Manuscript Online	2016-02-25 19:30

ISSN	1949-8454 (online)
Open Access	Open-Access: This article is an open-access article which was selected by an in-house editor and fully peer-reviewed by external reviewers. It is distributed in accordance with the Creative Commons Attribution Non Commercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original is properly cited and the use is non-commercial. See: http://creativecommons.org/licenses/by-nc/4.0/
Copyright	© The Author(s) 2016. Published by Baishideng Publishing Group Inc. All rights reserved.
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Category	Oncology
Manuscript Type	Minireviews
Article Title	API2-MALT1 oncoprotein promotes lymphomagenesis via unique program of substrate ubiquitination and proteolysis
Manuscript Source	Invited Manuscript
All Author List	Shaun Rosebeck, Megan S Lim, Kojo SJ Elenitoba-Johnson, Linda M McAllister-Lucas and Peter C Lucas
Funding Agency and Grant Number
Corresponding Author	Peter C Lucas, MD, PhD, Department of Pathology and Pediatrics, University of Pittsburgh School of Medicine, Pittsburgh, PA 15224, United States. lucaspc@upmc.edu
Key Words	Oncogene; Fusion oncoprotein; Lymphoma; Chromosomal translocation; Ubiquitination; Apoptosis; Nuclear factor-κB; Caspases
Core Tip	We summarize the identification of novel API2-mucosa-associated lymphoid tissue (MALT) 1-interacting proteins that uniquely mediate the cellular effects of the fusion oncoprotein but not wild-type API2 or MALT1. API2-MALT1 recruits receptor interacting protein 1 and tumor necrosis factor (TNF) receptor associated factor 2, which normally function downstream of the TNF receptor, and utilizes these proteins to communicate unregulated canonical nuclear factor-κB (NF-κB) in a manner that does not depend on the protease activity of MALT1. Simultaneously, NF-κB inducing kinase is recruited to API2-MALT1 and is proteolytically cleaved by the MALT1 protease domain to generate a stable, non-canonical NF-κB-activating fragment. Finally, LIM domain and actin-binding protein 1 is similarly recruited and cleaved as an API2-MALT1 specific target and its cleavage media-tes an NF-κB-independent mechanism of oncogenesis. Additional factors, including SMAC and BCL10, may also play key roles as API2-MALT1 binding partners and downstream signaling factors. Thus, the API2-MALT1 fusion utilizes a distinct set of protein-protein interactions to leverage multiple, divergent mechanisms and achieve potent oncogenic reprogramming of affected B cells.
Publish Date	2016-02-25 19:30
Citation	Rosebeck S, Lim MS, Elenitoba-Johnson KSJ, McAllister-Lucas LM, Lucas PC. API2-MALT1 oncoprotein promotes lymphomagenesis via unique program of substrate ubiquitination and proteolysis. World J Biol Chem 2016; 7(1): 128-137
URL	http://www.wjgnet.com/1949-8454/full/v7/i1/128.htm
DOI	http://dx.doi.org/10.4331/wjbc.v7.i1.128

Full Article (PDF)	WJBC-7-128.pdf
Full Article (Word)	WJBC-7-128.doc
Manuscript File	21390-Review.docx
Answering Reviewers	21390-Answering reviewers.pdf
Audio Core Tip	21390-Audio core tip.mp3
Conflict-of-Interest Disclosure Form	21390-Conflict-of-interest statement.pdf
Copyright License Agreement	21390-Copyright assignment.pdf
Peer-review Report	21390-Peer-review(s).pdf
Journal Editor-in-Chief Review Report	21390-Journal editor-in-chief review report.pdf
Scientific Misconduct Check	21390-Scientific misconduct check.pdf
Scientific Editor Work List	21390-Scientific editor work list.pdf