HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: M500112-MCP200v1 4/12/1898    most recent Submit a response Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Glossary Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Miles, R. R. Articles by Elenitoba-Johnson, K. S. J. Search for Related Content PubMed PubMed Citation Articles by Miles, R. R. Articles by Elenitoba-Johnson, K. S. J. Social Bookmarking                      What's this?

Molecular & Cellular Proteomics 4:1898-1909, 2005.
© 2005 by The American Society for Biochemistry and Molecular Biology, Inc.

---

Research

Analysis of BCL6-interacting Proteins by Tandem Mass Spectrometry^*,S

Rodney R. Miles^,, David K. Crockett^,¶, Megan S. Lim^,¶,|| and Kojo S. J. Elenitoba-Johnson^,¶,**

From the Department of Pathology, University of Utah School of Medicine, Salt Lake City, Utah 84132 and the ^¶ ARUP Institute for Clinical and Experimental Pathology, Salt Lake City, Utah 84108

B-cell lymphoma 6 (BCL6) is a 95-kDa nuclear phosphoprotein and member of the Pox virus zinc finger/bric-a-brac, tramtrack, broad complex (POZ/BTB) family of transcription factors. BCL6 is a transcriptional repressor required for germinal center formation, and the gene encoding it is frequently altered in diffuse large B-cell and follicular lymphomas. The dysregulation of BCL6 has therefore been implicated in lymphomagenesis. A limited number of proteins is known to interact with BCL6 and modulate its activity or participate in its role in transcriptional regulation. Identification of additional BCL6-binding proteins could reveal potential signaling targets and previously undescribed functional roles for BCL6. We used a functional proteomic approach to determine the identity of proteins that interact with BCL6. Proteins were isolated by co-immunoprecipitation with an anti-BCL6 antibody and identified using MS/MS. We identified 61 proteins in the BCL6 immunocomplex from the following Gene Ontology categories: transcription regulator activity (n = 18), binding activity (n = 11), signal transducer activity (n = 10), catalytic activity (n = 8), structural molecule activity (n = 3), enzyme regulator activity (n = 3), transporter activity (n = 2), motor activity (n = 2), chaperone activity (n = 1), and unknown function (n = 3). Importantly we identified BCL6 and several previously reported BCL6-interacting proteins in the BCL6 immunocomplex. The remaining proteins have not been shown previously to be associated with BCL6. MS/MS results were validated on four proteins using immunoprecipitation and Western blotting. Two of these protein interactions were further confirmed by reciprocal immunoprecipitation. This study demonstrates the utility of antibody immunoprecipitation and subsequent peptide identification by MS/MS for the elucidation of BCL6-binding proteins. Many of the novel proteins identified in this study suggest additional functional roles for BCL6 beyond transcriptional repression.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				T. Kuwata and T. Nakamura BCL11A is a SUMOylated protein and recruits SUMO-conjugation enzymes in its nuclear body Genes Cells, September 1, 2008; 13(9): 931 - 940. [Abstract] [Full Text] [PDF]

				S. Parekh, J. M. Polo, R. Shaknovich, P. Juszczynski, P. Lev, S. M. Ranuncolo, Y. Yin, U. Klein, G. Cattoretti, R. D. Favera, et al. BCL6 programs lymphoma cells for survival and differentiation through distinct biochemical mechanisms Blood, September 15, 2007; 110(6): 2067 - 2074. [Abstract] [Full Text] [PDF]