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: M700439-MCP200v1 7/7/1225    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 Request Permissions Glossary Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Moreira, J. M. A. Articles by Celis, J. E. Search for Related Content PubMed PubMed Citation Articles by Moreira, J. M. A. Articles by Celis, J. E. Social Bookmarking                      What's this?

Molecular & Cellular Proteomics 7:1225-1240, 2008.
© 2008 by The American Society for Biochemistry and Molecular Biology, Inc.

---

Research

A Combined Proteome and Ultrastructural Localization Analysis of 14-3-3 Proteins in Transformed Human Amnion (AMA) Cells

Definition of A Framework to Study Isoform-Specific Differences^*,S

José M. A. Moreira^,, Tao Shen^,¶, Gita Ohlsson^,||, Pavel Gromov, Irina Gromova and Julio E. Celis

From the Department of Proteomics in Cancer, Institute of Cancer Biology and Danish Centre for Translational Breast Cancer Research (DCTB), Danish Cancer Society, DK-2100 Copenhagen, Denmark and ^¶ Institute of Basic Medical Sciences, The First People's Hospital of Yunnan, Kunming 650032, China

The 14-3-3 proteins constitute a family of highly conserved and broadly expressed multifunctional polypeptides that are involved in a variety of important cellular processes that include cell cycle progression, growth, differentiation, and apoptosis. Although the exact cellular function(s) of 14-3-3 proteins is not fully elucidated, as a rule these proteins act by binding to protein ligands, thus regulating their activity; so far more than 300 cellular proteins have been reported to interact with 14-3-3 proteins. Binding to cognate interacting partners is isoform-specific, but redundancy also exists as several binding peptides can be recognized by all isoforms, and some functions can be carried out by any isoform indistinctly. Moreover by interacting with different ligands in a spatially and temporally regulated fashion the same isoform can play multiple possibly even opposing roles where the resultant cellular outcome will be determined by the integration of the various effects. Although there is a large body of literature on specific aspects of 14-3-3 biology, not much is known on the coordinated aspects of 14-3-3 isoform expression, post-translational modifications, and subcellular localization. To address the question of isoform-specific differences, we carried out a comparative analysis of the patterns of expression, phosphorylation, and subcellular localization of the 14-3-3 β, , , , and protein isoforms in transformed human amnion (AMA) cells. To validate as well as broaden our observations we analyzed the occurrence of the various isoforms in a large number of established cell lines and mammary and urothelial tissue specimens. Given the systematic approach we undertook and our application of isoform-discriminating technologies to the analysis of various cellular systems, we expect the data presented in this study to serve as an enabling resource for researchers working with 14-3-3 proteins.

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

This article has been cited by other articles:

				O. Halskau Jr., M. Ying, A. Baumann, R. Kleppe, D. Rodriguez-Larrea, B. Almas, J. Haavik, and A. Martinez Three-way Interaction between 14-3-3 Proteins, the N-terminal Region of Tyrosine Hydroxylase, and Negatively Charged Membranes J. Biol. Chem., November 20, 2009; 284(47): 32758 - 32769. [Abstract] [Full Text] [PDF]